Biological Process stringlengths 7 1.01k | Cellular Component stringlengths 6 867 | Molecular Function stringlengths 11 871 | Organism stringlengths 8 73 | Keywords stringlengths 1 810 | Sequence 10 stringlengths 5 10 | Sequence stringlengths 5 1.02k | Combined stringlengths 136 3.91k |
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cytoplasmic translation ribosomal large subunit assembly | cytoplasm; cytosolic large ribosomal subunit | rRNA binding structural constituent of ribosome tRNA binding | Escherichia coli | 3D-structure Direct protein sequencing Hydroxylation Methylation Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding tRNA-binding | MLQPKRTKFR | MLQPKRTKFRKMHKGRNRGLAQGTDVSFGSFGLKAVGRGRLTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLAVRMGKGKGNVEYWVALIQPGKVLYEMDGVPEELAREAFKLAAAKLPIKTTFVTKTVM | cytoplasmic translation ribosomal large subunit assembly cytoplasm; cytosolic large ribosomal subunit rRNA binding structural constituent of ribosome tRNA binding Escherichia coli 3D-structure Direct protein sequencing Hydroxylation Methylation Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding tRNA-binding MLQPKRTKFR MLQPKRTKFRKMHKGRNRGLAQGTDVSFGSFGLKAVGRGRLTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLAVRMGKGKGNVEYWVALIQPGKVLYEMDGVPEELAREAFKLAAAKLPIKTTFVTKTVM |
cytoplasmic translation ribosomal large subunit assembly | cytoplasm; cytosolic large ribosomal subunit | rRNA binding structural constituent of ribosome | Escherichia coli | 3D-structure Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding | MIREERLLKV | MIREERLLKVLRAPHVSEKASTAMEKSNTIVLKVAKDATKAEIKAAVQKLFEVEVEVVNTLVVKGKVKRHGQRIGRRSDWKKAYVTLKEGQNLDFVGGAE | cytoplasmic translation ribosomal large subunit assembly cytoplasm; cytosolic large ribosomal subunit rRNA binding structural constituent of ribosome Escherichia coli 3D-structure Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding MIREERLLKV MIREERLLKVLRAPHVSEKASTAMEKSNTIVLKVAKDATKAEIKAAVQKLFEVEVEVVNTLVVKGKVKRHGQRIGRRSDWKKAYVTLKEGQNLDFVGGAE |
cytoplasmic translation ribosomal small subunit assembly translation | cytoplasm; cytosol; cytosolic small ribosomal subunit | mRNA base-pairing translational repressor activity rRNA binding small ribosomal subunit rRNA binding structural constituent of ribosome | Escherichia coli | 3D-structure Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding Translation regulation | MSLSTEATAK | MSLSTEATAKIVSEFGRDANDTGSTEVQVALLTAQINHLQGHFAEHKKDHHSRRGLLRMVSQRRKLLDYLKRKDVARYTQLIERLGLRR | cytoplasmic translation ribosomal small subunit assembly translation cytoplasm; cytosol; cytosolic small ribosomal subunit mRNA base-pairing translational repressor activity rRNA binding small ribosomal subunit rRNA binding structural constituent of ribosome Escherichia coli 3D-structure Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding Translation regulation MSLSTEATAK MSLSTEATAKIVSEFGRDANDTGSTEVQVALLTAQINHLQGHFAEHKKDHHSRRGLLRMVSQRRKLLDYLKRKDVARYTQLIERLGLRR |
tRNA nucleoside ribose methylation | cytosol | protein homodimerization activity RNA binding tRNA (uracil-2'-O-)-methyltransferase activity | Escherichia coli | 3D-structure Cytoplasm Methyltransferase Reference proteome S-adenosyl-L-methionine Transferase tRNA processing | MLQNIRIVLV | MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAHIVDTLDEALAGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEAANTPVALVFGRERVGLTNEELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLATQENGEQVEHEETPYPLVDDLERFYGHLEQTLLATGFIRENHPGQVMNKLRRLFTRARPESQELNILRGILASIEQQNKGNKAE | tRNA nucleoside ribose methylation cytosol protein homodimerization activity RNA binding tRNA (uracil-2'-O-)-methyltransferase activity Escherichia coli 3D-structure Cytoplasm Methyltransferase Reference proteome S-adenosyl-L-methionine Transferase tRNA processing MLQNIRIVLV MLQNIRIVLVETSHTGNMGSVARAMKTMGLTNLWLVNPLVKPDSQAIALAAGASDVIGNAHIVDTLDEALAGCSLVVGTSARSRTLPWPMLDPRECGLKSVAEAANTPVALVFGRERVGLTNEELQKCHYHVAIAANPEYSSLNLAMAVQVIAYEVRMAWLATQENGEQVEHEETPYPLVDDLERFYGHLEQTLLATGFIRENHPGQVMNKLRRLFTRARPESQELNILRGILASIEQQNKGNKAE |
bile acid and bile salt transport response to antibiotic xenobiotic detoxification by transmembrane export across the cell outer membrane xenobiotic transport | efflux pump complex; outer membrane-bounded periplasmic space; periplasmic side of plasma membrane | identical protein binding transmembrane transporter activity | Escherichia coli | 3D-structure Antibiotic resistance Cell inner membrane Cell membrane Coiled coil Lipoprotein Membrane Palmitate Reference proteome Signal Transport | MNKNRGFTPL | MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS | bile acid and bile salt transport response to antibiotic xenobiotic detoxification by transmembrane export across the cell outer membrane xenobiotic transport efflux pump complex; outer membrane-bounded periplasmic space; periplasmic side of plasma membrane identical protein binding transmembrane transporter activity Escherichia coli 3D-structure Antibiotic resistance Cell inner membrane Cell membrane Coiled coil Lipoprotein Membrane Palmitate Reference proteome Signal Transport MNKNRGFTPL MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS |
cell redox homeostasis cellular response to sulfate starvation hydrogen peroxide catabolic process response to alkyl hydroperoxide response to hydroperoxide response to oxidative stress siderophore biosynthetic process | alkyl hydroperoxide reductase complex; cytoplasm; cytosol; membrane | hydroperoxide reductase activity identical protein binding NADH-dependent peroxiredoxin activity oxidoreductase activity, acting on peroxide as acceptor peroxidase activity thioredoxin peroxidase activity | Escherichia coli | 3D-structure Acetylation Antioxidant Cytoplasm Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome | MSLINTKIKP | MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPSLDLVGKI | cell redox homeostasis cellular response to sulfate starvation hydrogen peroxide catabolic process response to alkyl hydroperoxide response to hydroperoxide response to oxidative stress siderophore biosynthetic process alkyl hydroperoxide reductase complex; cytoplasm; cytosol; membrane hydroperoxide reductase activity identical protein binding NADH-dependent peroxiredoxin activity oxidoreductase activity, acting on peroxide as acceptor peroxidase activity thioredoxin peroxidase activity Escherichia coli 3D-structure Acetylation Antioxidant Cytoplasm Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome MSLINTKIKP MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPSLDLVGKI |
AMP salvage nucleoside metabolic process | cytosol | AMP nucleosidase activity | Escherichia coli | 3D-structure Allosteric enzyme Direct protein sequencing Hydrolase Reference proteome | MNNKGSGLTP | MNNKGSGLTPAQALDKLDALYEQSVVALRNAIGNYITSGELPDENARKQGLFVYPSLTVTWDGSTTNPPKTRAFGRFTHAGSYTTTITRPTLFRSYLNEQLTLLYQDYGAHISVQPSQHEIPYPYVIDGSELTLDRSMSAGLTRYFPTTELAQIGDETADGIYHPTEFSPLSHFDARRVDFSLARLRHYTGTPVEHFQPFVLFTNYTRYVDEFVRWGCSQILDPDSPYIALSCAGGNWITAETEAPEEAISDLAWKKHQMPAWHLITADGQGITLVNIGVGPSNAKTICDHLAVLRPDVWLMIGHCGGLRESQAIGDYVLAHAYLRDDHVLDAVLPPDIPIPSIAEVQRALYDATKLVSGRPGEEVKQRLRTGTVVTTDDRNWELRYSASALRFNLSRAVAIDMESATIAAQGYRFRVPYGTLLCVSDKPLHGEIKLPGQANRFYEGAISEHLQIGIRAIDLLRAEGDRLHSRKLRTFNEPPFR | AMP salvage nucleoside metabolic process cytosol AMP nucleosidase activity Escherichia coli 3D-structure Allosteric enzyme Direct protein sequencing Hydrolase Reference proteome MNNKGSGLTP MNNKGSGLTPAQALDKLDALYEQSVVALRNAIGNYITSGELPDENARKQGLFVYPSLTVTWDGSTTNPPKTRAFGRFTHAGSYTTTITRPTLFRSYLNEQLTLLYQDYGAHISVQPSQHEIPYPYVIDGSELTLDRSMSAGLTRYFPTTELAQIGDETADGIYHPTEFSPLSHFDARRVDFSLARLRHYTGTPVEHFQPFVLFTNYTRYVDEFVRWGCSQILDPDSPYIALSCAGGNWITAETEAPEEAISDLAWKKHQMPAWHLITADGQGITLVNIGVGPSNAKTICDHLAVLRPDVWLMIGHCGGLRESQAIGDYVLAHAYLRDDHVLDAVLPPDIPIPSIAEVQRALYDATKLVSGRPGEEVKQRLRTGTVVTTDDRNWELRYSASALRFNLSRAVAIDMESATIAAQGYRFRVPYGTLLCVSDKPLHGEIKLPGQANRFYEGAISEHLQIGIRAIDLLRAEGDRLHSRKLRTFNEPPFR |
proteolysis | cytosol | ferrous iron binding initiator methionyl aminopeptidase activity metalloaminopeptidase activity | Escherichia coli | 3D-structure Aminopeptidase Direct protein sequencing Hydrolase Metal-binding Protease Reference proteome | MAISIKTPED | MAISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE | proteolysis cytosol ferrous iron binding initiator methionyl aminopeptidase activity metalloaminopeptidase activity Escherichia coli 3D-structure Aminopeptidase Direct protein sequencing Hydrolase Metal-binding Protease Reference proteome MAISIKTPED MAISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE |
fucose transmembrane transport L-arabinose transmembrane transport transmembrane transport | membrane; plasma membrane | fucose transmembrane transporter activity L-arabinose transmembrane transporter activity symporter activity | Escherichia coli | Cell inner membrane Cell membrane Membrane Reference proteome Sugar transport Symport Transmembrane Transmembrane helix Transport | MVTINTESAL | MVTINTESALTPRSLRDTRRMNMFVSVAAAVAGLLFGLDIGVIAGALPFITDHFVLTSRLQEWVVSSMMLGAAIGALFNGWLSFRLGRKYSLMAGAILFVLGSIGSAFATSVEMLIAARVVLGIAVGIASYTAPLYLSEMASENVRGKMISMYQLMVTLGIVLAFLSDTAFSYSGNWRAMLGVLALPAVLLIILVVFLPNSPRWLAEKGRHIEAEEVLRMLRDTSEKAREELNEIRESLKLKQGGWALFKINRNVRRAVFLGMLLQAMQQFTGMNIIMYYAPRIFKMAGFTTTEQQMIATLVVGLTFMFATFIAVFTVDKAGRKPALKIGFSVMALGTLVLGYCLMQFDNGTASSGLSWLSVGMTMMCIAGYAMSAAPVVWILCSEIQPLKCRDFGITCSTTTNWVSNMIIGATFLTLLDSIGAAGTFWLYTALNIAFVGITFWLIPETKNVTLEHIERKLMAGEKLRNIGV | fucose transmembrane transport L-arabinose transmembrane transport transmembrane transport membrane; plasma membrane fucose transmembrane transporter activity L-arabinose transmembrane transporter activity symporter activity Escherichia coli Cell inner membrane Cell membrane Membrane Reference proteome Sugar transport Symport Transmembrane Transmembrane helix Transport MVTINTESAL MVTINTESALTPRSLRDTRRMNMFVSVAAAVAGLLFGLDIGVIAGALPFITDHFVLTSRLQEWVVSSMMLGAAIGALFNGWLSFRLGRKYSLMAGAILFVLGSIGSAFATSVEMLIAARVVLGIAVGIASYTAPLYLSEMASENVRGKMISMYQLMVTLGIVLAFLSDTAFSYSGNWRAMLGVLALPAVLLIILVVFLPNSPRWLAEKGRHIEAEEVLRMLRDTSEKAREELNEIRESLKLKQGGWALFKINRNVRRAVFLGMLLQAMQQFTGMNIIMYYAPRIFKMAGFTTTEQQMIATLVVGLTFMFATFIAVFTVDKAGRKPALKIGFSVMALGTLVLGYCLMQFDNGTASSGLSWLSVGMTMMCIAGYAMSAAPVVWILCSEIQPLKCRDFGITCSTTTNWVSNMIIGATFLTLLDSIGAAGTFWLYTALNIAFVGITFWLIPETKNVTLEHIERKLMAGEKLRNIGV |
cell redox homeostasis cellular response to oxidative stress response to oxidative stress | cytoplasm; cytosol | hydroperoxide reductase activity thioredoxin peroxidase activity | Escherichia coli | Antioxidant Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome | MNPLKAGDIA | MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVDVLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKSFMGKTYDGIHRISFLIDADGKIEHVFDDFKTSNHHDVVLNWLKEHA | cell redox homeostasis cellular response to oxidative stress response to oxidative stress cytoplasm; cytosol hydroperoxide reductase activity thioredoxin peroxidase activity Escherichia coli Antioxidant Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome MNPLKAGDIA MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVDVLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKSFMGKTYDGIHRISFLIDADGKIEHVFDDFKTSNHHDVVLNWLKEHA |
aerotaxis bacterial-type flagellum-dependent swimming motility chemotaxis internal peptidyl-lysine acetylation phosphorelay signal transduction system regulation of bacterial-type flagellum-dependent cell motility regulation of chemotaxis signal transduction thermotaxis | bacterial-type flagellum; bacterial-type flagellum basal body, C ring; bacterial-type flagellum rotor complex; cytoplasm; cytosol | acetyltransferase activity magnesium ion binding phosphorelay response regulator activity | Escherichia coli | 3D-structure Acetylation Chemotaxis Cytoplasm Direct protein sequencing Flagellar rotation Magnesium Metal-binding Phosphoprotein Reference proteome Two-component regulatory system | MADKELKFLV | MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM | aerotaxis bacterial-type flagellum-dependent swimming motility chemotaxis internal peptidyl-lysine acetylation phosphorelay signal transduction system regulation of bacterial-type flagellum-dependent cell motility regulation of chemotaxis signal transduction thermotaxis bacterial-type flagellum; bacterial-type flagellum basal body, C ring; bacterial-type flagellum rotor complex; cytoplasm; cytosol acetyltransferase activity magnesium ion binding phosphorelay response regulator activity Escherichia coli 3D-structure Acetylation Chemotaxis Cytoplasm Direct protein sequencing Flagellar rotation Magnesium Metal-binding Phosphoprotein Reference proteome Two-component regulatory system MADKELKFLV MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM |
defense response to virus mRNA catabolic process negative regulation of cell growth positive regulation of programmed cell death quorum sensing regulation of DNA-templated transcription regulation of growth regulation of translation rRNA catabolic process single-species biofilm formation | protein-containing complex; toxin-antitoxin complex | DNA binding molecular function activator activity protein homodimerization activity protein-containing complex binding RNA binding RNA endonuclease activity | Escherichia coli | 3D-structure ADP-ribosylation Antiviral defense DNA-binding Endonuclease Hydrolase Nuclease Quorum sensing Reference proteome Repressor RNA-binding Stress response Toxin-antitoxin system Transcription Transcription regulation Translation regulation | MVSRYVPDMG | MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG | defense response to virus mRNA catabolic process negative regulation of cell growth positive regulation of programmed cell death quorum sensing regulation of DNA-templated transcription regulation of growth regulation of translation rRNA catabolic process single-species biofilm formation protein-containing complex; toxin-antitoxin complex DNA binding molecular function activator activity protein homodimerization activity protein-containing complex binding RNA binding RNA endonuclease activity Escherichia coli 3D-structure ADP-ribosylation Antiviral defense DNA-binding Endonuclease Hydrolase Nuclease Quorum sensing Reference proteome Repressor RNA-binding Stress response Toxin-antitoxin system Transcription Transcription regulation Translation regulation MVSRYVPDMG MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG |
regulation of DNA-templated transcription regulation of growth single-species biofilm formation | protein-containing complex; toxin-antitoxin complex | double-stranded DNA binding protein homodimerization activity protein-containing complex binding toxin sequestering activity | Escherichia coli | 3D-structure DNA-binding Reference proteome Repressor Toxin-antitoxin system Transcription Transcription regulation | MIHSSVKRWG | MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW | regulation of DNA-templated transcription regulation of growth single-species biofilm formation protein-containing complex; toxin-antitoxin complex double-stranded DNA binding protein homodimerization activity protein-containing complex binding toxin sequestering activity Escherichia coli 3D-structure DNA-binding Reference proteome Repressor Toxin-antitoxin system Transcription Transcription regulation MIHSSVKRWG MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW |
cell adhesion involved in biofilm formation cellular response to cell envelope stress response to radiation signal transduction | plasma membrane | ATP binding identical protein binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity | Escherichia coli | 3D-structure ATP-binding Cell adhesion Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system | MIGSLTARIF | MIGSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHVEAELANDPPNDLMWWRRLFRAIDKWAPPGQRLLLVTTEGRVIGAERSEMQIIRNFIGQADNADHPQKKKYGRVELVGPFSVRDGEDNYQLYLIRPASSSQSDFINLLFDRPLLLLIVTMLVSTPLLLWLAWSLAKPARKLKNAADEVAQGNLRQHPELEAGPQEFLAAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLGTALLRRRSGESKELERIETEAQRLDSMINDLLVMSRNQQKNALVSETIKANQLWSEVLDNAAFEAEQMGKSLTVNFPPGPWPLYGNPNALESALENIVRNALRYSHTKIEVGFAVDKDGITITVDDDGPGVSPEDREQIFRPFYRTDEARDRESGGTGLGLAIVETAIQQHRGWVKAEDSPLGGLRLVIWLPLYKRS | cell adhesion involved in biofilm formation cellular response to cell envelope stress response to radiation signal transduction plasma membrane ATP binding identical protein binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity Escherichia coli 3D-structure ATP-binding Cell adhesion Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system MIGSLTARIF MIGSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHVEAELANDPPNDLMWWRRLFRAIDKWAPPGQRLLLVTTEGRVIGAERSEMQIIRNFIGQADNADHPQKKKYGRVELVGPFSVRDGEDNYQLYLIRPASSSQSDFINLLFDRPLLLLIVTMLVSTPLLLWLAWSLAKPARKLKNAADEVAQGNLRQHPELEAGPQEFLAAGASFNQMVTALERMMTSQQRLLSDISHELRTPLTRLQLGTALLRRRSGESKELERIETEAQRLDSMINDLLVMSRNQQKNALVSETIKANQLWSEVLDNAAFEAEQMGKSLTVNFPPGPWPLYGNPNALESALENIVRNALRYSHTKIEVGFAVDKDGITITVDDDGPGVSPEDREQIFRPFYRTDEARDRESGGTGLGLAIVETAIQQHRGWVKAEDSPLGGLRLVIWLPLYKRS |
cell adhesion negative regulation of DNA-templated transcription positive regulation of DNA-templated transcription regulation of cell-substrate adhesion regulation of DNA-templated transcription | cytosol; protein-DNA complex | DNA-binding transcription factor activity phosphorelay response regulator activity transcription cis-regulatory region binding | Escherichia coli | 3D-structure Activator Cell adhesion Cytoplasm DNA-binding Phosphoprotein Reference proteome Stress response Transcription Transcription regulation Two-component regulatory system | MNKILLVDDD | MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKALRQTHQTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEVDALVLNPGRQEASFDGQTLELTGTEFTLLYLLAQHLGQVVSREHLSQEVLGKRLTPFDRAIDMHISNLRRKLPDRKDGHPWFKTLRGRGYLMVSAS | cell adhesion negative regulation of DNA-templated transcription positive regulation of DNA-templated transcription regulation of cell-substrate adhesion regulation of DNA-templated transcription cytosol; protein-DNA complex DNA-binding transcription factor activity phosphorelay response regulator activity transcription cis-regulatory region binding Escherichia coli 3D-structure Activator Cell adhesion Cytoplasm DNA-binding Phosphoprotein Reference proteome Stress response Transcription Transcription regulation Two-component regulatory system MNKILLVDDD MNKILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDLLLLDVMMPKKNGIDTLKALRQTHQTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSHWSEQQQNNDNGSPTLEVDALVLNPGRQEASFDGQTLELTGTEFTLLYLLAQHLGQVVSREHLSQEVLGKRLTPFDRAIDMHISNLRRKLPDRKDGHPWFKTLRGRGYLMVSAS |
cell wall organization peptidoglycan biosynthetic process peptidoglycan metabolic process proteolysis regulation of cell shape | outer membrane-bounded periplasmic space; plasma membrane | beta-lactamase activity carboxypeptidase activity penicillin binding protein homodimerization activity serine-type D-Ala-D-Ala carboxypeptidase activity | Escherichia coli | 3D-structure Carboxypeptidase Cell inner membrane Cell membrane Cell shape Cell wall biogenesis/degradation Direct protein sequencing Hydrolase Membrane Peptidoglycan synthesis Protease Reference proteome Signal | MNTIFSARIM | MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG | cell wall organization peptidoglycan biosynthetic process peptidoglycan metabolic process proteolysis regulation of cell shape outer membrane-bounded periplasmic space; plasma membrane beta-lactamase activity carboxypeptidase activity penicillin binding protein homodimerization activity serine-type D-Ala-D-Ala carboxypeptidase activity Escherichia coli 3D-structure Carboxypeptidase Cell inner membrane Cell membrane Cell shape Cell wall biogenesis/degradation Direct protein sequencing Hydrolase Membrane Peptidoglycan synthesis Protease Reference proteome Signal MNTIFSARIM MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG |
protein autophosphorylation regulation of DNA-templated transcription response to oxygen levels signal transduction | cytosol; plasma membrane | ATP binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity | Escherichia coli | 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Transferase Transmembrane Transmembrane helix Two-component regulatory system | MKQIRLLAQY | MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFGQLKIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPADVYSPEAAAKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFLADLENLSALQAQQKGLRFNLEPTLPLPHQVITDGTRLRQILWNLISNAVKFTQQGQVTVRVRYDEGDMLHFEVEDSGIGIPQDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSRRLAKNMGGDITVTSEQGKGSTFTLTIHAPSVAEEVDDAFDEDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTKRYPREDLPPLVALTANVLKDKQEYLNAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVTTEENSKSEALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYVSVLESNLTAQDKKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKEEWRHDVEVLKAWVAKATKK | protein autophosphorylation regulation of DNA-templated transcription response to oxygen levels signal transduction cytosol; plasma membrane ATP binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity Escherichia coli 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Transferase Transmembrane Transmembrane helix Two-component regulatory system MKQIRLLAQY MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIFFGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIAVREKAEAELQETFGQLKIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGCNRAMELLTGKSEKQLVHLKPADVYSPEAAAKVIETDEKVFRHNVSLTYEQWLDYPDGRKACFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTSFLADLENLSALQAQQKGLRFNLEPTLPLPHQVITDGTRLRQILWNLISNAVKFTQQGQVTVRVRYDEGDMLHFEVEDSGIGIPQDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSRRLAKNMGGDITVTSEQGKGSTFTLTIHAPSVAEEVDDAFDEDDMPLPALNVLLVEDIELNVIVARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTKRYPREDLPPLVALTANVLKDKQEYLNAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVTTEENSKSEALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYVSVLESNLTAQDKKGIVEEGHKIKGAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKEEWRHDVEVLKAWVAKATKK |
response to acetate response to formic acid response to hydrogen peroxide | plasma membrane | ATP binding histidine phosphotransfer kinase activity phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein histidine kinase activity protein homodimerization activity | Escherichia coli | ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Transferase Transmembrane Transmembrane helix Two-component regulatory system | MTNYSLRARM | MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETPLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVNEIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG | response to acetate response to formic acid response to hydrogen peroxide plasma membrane ATP binding histidine phosphotransfer kinase activity phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein histidine kinase activity protein homodimerization activity Escherichia coli ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Transferase Transmembrane Transmembrane helix Two-component regulatory system MTNYSLRARM MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGMSLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQLTVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFISSVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGINSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLILESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNAIKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLAYVEPNSAAAQCTLDILSETPLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLAKAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQNTLLPVTDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQMPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNLLLRYKPGSGISSRVVTPEVNEIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEVRNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSGTKEEDLEPELLELLDEMDNVAREASKILG |
phosphorelay signal transduction system regulation of DNA-templated transcription signal transduction | cytosol; outer membrane-bounded periplasmic space; plasma membrane; protein histidine kinase complex | ATP binding identical protein binding phosphorelay sensor kinase activity protein histidine kinase activity | Escherichia coli | 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system | MRHSLPYRML | MRHSLPYRMLRKRPMKLSTTVILMVSAVLFSVLLVVHLIYFSQISDMTRDGLANKALAVARTLADSPEIRQGLQKKPQESGIQAIAEAVRKRNDLLFIVVTDMQSLRYSHPEAQRIGQPFKGDDILKALNGEENVAINRGFLAQALRVFTPIYDENHKQIGVVAIGLELSRVTQQINDSRWSIIWSVLFGMLVGLIGTCILVKVLKKILFGLEPYEISTLFEQRQAMLQSIKEGVVAVDDRGEVTLINDAAQELLNYRKSQDDEKLSTLSHSWSQVVDVSEVLRDGTPRRDEEITIKDRLLLINTVPVRSNGVIIGAISTFRDKTEVRKLMQRLDGLVNYADALRERSHEFMNKLHVILGLLHLKSYKQLEDYILKTANNYQEEIGSLLGKIKSPVIAGFLISKINRATDLGHTLILNSESQLPDSGSEDQVATLITTLGNLIENALEALGPEPGGEISVTLHYRHGWLHCEVNDDGPGIAPDKIDHIFDKGVSTKGSERGVGLALVKQQVENLGGSIAVESEPGIFTQFFVQIPWDGERSNR | phosphorelay signal transduction system regulation of DNA-templated transcription signal transduction cytosol; outer membrane-bounded periplasmic space; plasma membrane; protein histidine kinase complex ATP binding identical protein binding phosphorelay sensor kinase activity protein histidine kinase activity Escherichia coli 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system MRHSLPYRML MRHSLPYRMLRKRPMKLSTTVILMVSAVLFSVLLVVHLIYFSQISDMTRDGLANKALAVARTLADSPEIRQGLQKKPQESGIQAIAEAVRKRNDLLFIVVTDMQSLRYSHPEAQRIGQPFKGDDILKALNGEENVAINRGFLAQALRVFTPIYDENHKQIGVVAIGLELSRVTQQINDSRWSIIWSVLFGMLVGLIGTCILVKVLKKILFGLEPYEISTLFEQRQAMLQSIKEGVVAVDDRGEVTLINDAAQELLNYRKSQDDEKLSTLSHSWSQVVDVSEVLRDGTPRRDEEITIKDRLLLINTVPVRSNGVIIGAISTFRDKTEVRKLMQRLDGLVNYADALRERSHEFMNKLHVILGLLHLKSYKQLEDYILKTANNYQEEIGSLLGKIKSPVIAGFLISKINRATDLGHTLILNSESQLPDSGSEDQVATLITTLGNLIENALEALGPEPGGEISVTLHYRHGWLHCEVNDDGPGIAPDKIDHIFDKGVSTKGSERGVGLALVKQQVENLGGSIAVESEPGIFTQFFVQIPWDGERSNR |
diaminopimelate biosynthetic process lysine biosynthetic process via diaminopimelate | cell division site; cytosol | cobalt ion binding identical protein binding succinyl-diaminopimelate desuccinylase activity zinc ion binding | Escherichia coli | Amino-acid biosynthesis Cobalt Diaminopimelate biosynthesis Hydrolase Lysine biosynthesis Metal-binding Reference proteome Zinc | MSCPVIELTQ | MSCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA | diaminopimelate biosynthetic process lysine biosynthetic process via diaminopimelate cell division site; cytosol cobalt ion binding identical protein binding succinyl-diaminopimelate desuccinylase activity zinc ion binding Escherichia coli Amino-acid biosynthesis Cobalt Diaminopimelate biosynthesis Hydrolase Lysine biosynthesis Metal-binding Reference proteome Zinc MSCPVIELTQ MSCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA |
cellular response to misfolded protein proteolysis | outer membrane-bounded periplasmic space; plasma membrane | identical protein binding peptidase activity serine-type endopeptidase activity serine-type peptidase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Hydrolase Membrane Protease Reference proteome Serine protease Transmembrane Transmembrane helix | MFVKLLRSVA | MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN | cellular response to misfolded protein proteolysis outer membrane-bounded periplasmic space; plasma membrane identical protein binding peptidase activity serine-type endopeptidase activity serine-type peptidase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Hydrolase Membrane Protease Reference proteome Serine protease Transmembrane Transmembrane helix MFVKLLRSVA MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN |
chemotaxis galactose transmembrane transport methylgalactoside transport | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; membrane; outer membrane-bounded periplasmic space | calcium ion binding carbohydrate binding | Escherichia coli | 3D-structure Calcium Chemotaxis Direct protein sequencing Metal-binding Periplasm Reference proteome Signal Sugar transport Transport | MNKKVLTLSA | MNKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSKK | chemotaxis galactose transmembrane transport methylgalactoside transport ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; membrane; outer membrane-bounded periplasmic space calcium ion binding carbohydrate binding Escherichia coli 3D-structure Calcium Chemotaxis Direct protein sequencing Metal-binding Periplasm Reference proteome Signal Sugar transport Transport MNKKVLTLSA MNKKVLTLSAVMASMLFGAAAHAADTRIGVTIYKYDDNFMSVVRKAIEQDAKAAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGIIQGDLIAKHWAANQGWDLNKDGQIQFVLLKGEPGHPDAEARTTYVIKELNDKGIKTEQLQLDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGALAGTVLNDANNQAKATFDLAKNLADGKGAADGTNWKIDNKVVRVPYVGVDKDNLAEFSKK |
cellular response to antibiotic | outer membrane-bounded periplasmic space | protein disulfide isomerase activity protein-disulfide reductase activity | Escherichia coli | 3D-structure Direct protein sequencing Disulfide bond Periplasm Redox-active center Reference proteome Signal | MKKIWLALAG | MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK | cellular response to antibiotic outer membrane-bounded periplasmic space protein disulfide isomerase activity protein-disulfide reductase activity Escherichia coli 3D-structure Direct protein sequencing Disulfide bond Periplasm Redox-active center Reference proteome Signal MKKIWLALAG MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK |
chaperone-mediated protein folding response to copper ion | outer membrane-bounded periplasmic space; periplasmic space | protein disulfide isomerase activity protein homodimerization activity protein-disulfide reductase activity | Escherichia coli | 3D-structure Direct protein sequencing Disulfide bond Periplasm Redox-active center Reference proteome Signal | MKKGFMLFTL | MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYITDDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAPASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK | chaperone-mediated protein folding response to copper ion outer membrane-bounded periplasmic space; periplasmic space protein disulfide isomerase activity protein homodimerization activity protein-disulfide reductase activity Escherichia coli 3D-structure Direct protein sequencing Disulfide bond Periplasm Redox-active center Reference proteome Signal MKKGFMLFTL MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYITDDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAPASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK |
cellular response to cell envelope stress positive regulation of DNA-templated transcription proteolysis | plasma membrane | anti-sigma factor antagonist activity metal ion binding metalloendopeptidase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Hydrolase Membrane Metal-binding Metalloprotease Protease Reference proteome Repeat Transmembrane Transmembrane helix Zinc | MLSFLWDLAS | MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQYGPFNAIVEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAKGAGMTAELGVVYYLPFLALISVNLGIINLFPLPVLDGGHLLFLAIEKIKGGPVSERVQDFCYRIGSILLVLLMGLALFNDFSRL | cellular response to cell envelope stress positive regulation of DNA-templated transcription proteolysis plasma membrane anti-sigma factor antagonist activity metal ion binding metalloendopeptidase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Hydrolase Membrane Metal-binding Metalloprotease Protease Reference proteome Repeat Transmembrane Transmembrane helix Zinc MLSFLWDLAS MLSFLWDLASFIVALGVLITVHEFGHFWVARRCGVRVERFSIGFGKALWRRTDKLGTEYVIALIPLGGYVKMLDERAEPVVPELRHHAFNNKSVGQRAAIIAAGPVANFIFAIFAYWLVFIIGVPGVRPVVGEIAANSIAAEAQIAPGTELKAVDGIETPDWDAVRLQLVDKIGDESTTITVAPFGSDQRRDVKLDLRHWAFEPDKEDPVSSLGIRPRGPQIEPVLENVQPNSAASKAGLQAGDRIVKVDGQPLTQWVTFVMLVRDNPGKSLALEIERQGSPLSLTLIPESKPGNGKAIGFVGIEPKVIPLPDEYKVVRQYGPFNAIVEATDKTWQLMKLTVSMLGKLITGDVKLNNLSGPISIAKGAGMTAELGVVYYLPFLALISVNLGIINLFPLPVLDGGHLLFLAIEKIKGGPVSERVQDFCYRIGSILLVLLMGLALFNDFSRL |
tRNA methylation tRNA methylthiolation | cytosol | 4 iron, 4 sulfur cluster binding metal ion binding N6-isopentenyladenosine methylthiotransferase activity | Escherichia coli | 4Fe-4S Cytoplasm Iron Iron-sulfur Metal-binding Reference proteome S-adenosyl-L-methionine Transferase tRNA processing | MTKKLHIKTW | MTKKLHIKTWGCQMNEYDSSKMADLLDATHGYQLTDVAEEADVLLLNTCSIREKAQEKVFHQLGRWKLLKEKNPDLIIGVGGCVASQEGEHIRQRAHYVDIIFGPQTLHRLPEMINSVRGDRSPVVDISFPEIEKFDRLPEPRAEGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPSDDILFEIAQLAAQGVREVNLLGQNVNAWRGENYDGTTGSFADLLRLVAAIDGIDRIRFTTSHPIEFTDDIIEVYRDTPELVSFLHLPVQSGSDRILNLMGRTHTALEYKAIIRKLRAARPDIQISSDFIVGFPGETTEDFEKTMKLIADVNFDMSYSFIFSARPGTPAADMVDDVPEEEKKQRLYILQERINQQAMAWSRRMLGTTQRILVEGTSRKSIMELSGRTENNRVVNFEGTPDMIGKFVDVEITDVYPNSLRGKVVRTEDEMGLRVAETPESVIARTRKENDLGVGYYQP | tRNA methylation tRNA methylthiolation cytosol 4 iron, 4 sulfur cluster binding metal ion binding N6-isopentenyladenosine methylthiotransferase activity Escherichia coli 4Fe-4S Cytoplasm Iron Iron-sulfur Metal-binding Reference proteome S-adenosyl-L-methionine Transferase tRNA processing MTKKLHIKTW MTKKLHIKTWGCQMNEYDSSKMADLLDATHGYQLTDVAEEADVLLLNTCSIREKAQEKVFHQLGRWKLLKEKNPDLIIGVGGCVASQEGEHIRQRAHYVDIIFGPQTLHRLPEMINSVRGDRSPVVDISFPEIEKFDRLPEPRAEGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPSDDILFEIAQLAAQGVREVNLLGQNVNAWRGENYDGTTGSFADLLRLVAAIDGIDRIRFTTSHPIEFTDDIIEVYRDTPELVSFLHLPVQSGSDRILNLMGRTHTALEYKAIIRKLRAARPDIQISSDFIVGFPGETTEDFEKTMKLIADVNFDMSYSFIFSARPGTPAADMVDDVPEEEKKQRLYILQERINQQAMAWSRRMLGTTQRILVEGTSRKSIMELSGRTENNRVVNFEGTPDMIGKFVDVEITDVYPNSLRGKVVRTEDEMGLRVAETPESVIARTRKENDLGVGYYQP |
phosphorelay signal transduction system phosphorylation protein autophosphorylation response to osmotic stress signal transduction | cytosol; outer membrane-bounded periplasmic space; plasma membrane | ATP binding identical protein binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein homodimerization activity | Escherichia coli | 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Stress response Transferase Transmembrane Transmembrane helix Two-component regulatory system | MRRLRFSPRS | MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG | phosphorelay signal transduction system phosphorylation protein autophosphorylation response to osmotic stress signal transduction cytosol; outer membrane-bounded periplasmic space; plasma membrane ATP binding identical protein binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein homodimerization activity Escherichia coli 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Stress response Transferase Transmembrane Transmembrane helix Two-component regulatory system MRRLRFSPRS MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIETALYPGSIEVKMHPLSIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPVPVTRAQGTTKEG |
amino acid metabolic process ethanolamine catabolic process | cytosol; ethanolamine ammonia-lyase complex; ethanolamine degradation polyhedral organelle | cobalamin binding ethanolamine ammonia-lyase activity | Escherichia coli | 3D-structure Bacterial microcompartment Cobalamin Cobalt Direct protein sequencing Lyase Reference proteome | MKLKTTLFGN | MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTTIGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVENLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANFGADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHFMGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDIMLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPSLFF | amino acid metabolic process ethanolamine catabolic process cytosol; ethanolamine ammonia-lyase complex; ethanolamine degradation polyhedral organelle cobalamin binding ethanolamine ammonia-lyase activity Escherichia coli 3D-structure Bacterial microcompartment Cobalamin Cobalt Direct protein sequencing Lyase Reference proteome MKLKTTLFGN MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTTIGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVENLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANFGADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHFMGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDIMLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPSLFF |
biotin biosynthetic process fatty acid biosynthetic process fatty acid elongation lipid biosynthetic process | cytosol | 3-oxoacyl- reductase (NADPH) activity identical protein binding metal ion binding NAD binding NADP binding oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | Escherichia coli | 3D-structure Calcium Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Metal-binding NADP Oxidoreductase Reference proteome | MNFEGKIALV | MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV | biotin biosynthetic process fatty acid biosynthetic process fatty acid elongation lipid biosynthetic process cytosol 3-oxoacyl- reductase (NADPH) activity identical protein binding metal ion binding NAD binding NADP binding oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Escherichia coli 3D-structure Calcium Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Metal-binding NADP Oxidoreductase Reference proteome MNFEGKIALV MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNVTDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKAVMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVAPGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGGMYMV |
biotin biosynthetic process fatty acid elongation lipid biosynthetic process protein homotetramerization response to antibiotic | catalytic complex; cytosol; membrane; protein-containing complex | enoyl- reductase (NADH) activity enoyl- reductase activity identical protein binding NADH binding | Escherichia coli | 3D-structure Antibiotic resistance Direct protein sequencing Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism NAD Oxidoreductase Reference proteome | MGFLSGKRIL | MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK | biotin biosynthetic process fatty acid elongation lipid biosynthetic process protein homotetramerization response to antibiotic catalytic complex; cytosol; membrane; protein-containing complex enoyl- reductase (NADH) activity enoyl- reductase activity identical protein binding NADH binding Escherichia coli 3D-structure Antibiotic resistance Direct protein sequencing Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism NAD Oxidoreductase Reference proteome MGFLSGKRIL MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK |
chaperone-mediated protein folding | cytosol | peptidyl-prolyl cis-trans isomerase activity | Escherichia coli | 3D-structure Isomerase Reference proteome Rotamase | MSESVQSNSA | MSESVQSNSAVLVHFTLKLDDGTTAESTRNNGKPALFRLGDASLSEGLEQHLLGLKVGDKTTFSLEPDAAFGVPSPDLIQYFSRREFMDAGEPEIGAIMLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEA | chaperone-mediated protein folding cytosol peptidyl-prolyl cis-trans isomerase activity Escherichia coli 3D-structure Isomerase Reference proteome Rotamase MSESVQSNSA MSESVQSNSAVLVHFTLKLDDGTTAESTRNNGKPALFRLGDASLSEGLEQHLLGLKVGDKTTFSLEPDAAFGVPSPDLIQYFSRREFMDAGEPEIGAIMLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEA |
bacterial-type flagellum assembly bacterial-type flagellum-dependent cell motility DNA-templated transcription initiation regulation of DNA-templated transcription regulation of DNA-templated transcription initiation | cytosol; cytosolic DNA-directed RNA polymerase complex | DNA binding DNA-directed 5'-3' RNA polymerase activity sigma factor activity | Escherichia coli | 3D-structure Cytoplasm DNA-binding Reference proteome Sigma factor Transcription Transcription regulation | MNSLYTAEGV | MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVERYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAIGQLEQELGRNATETEVAERLGIDIADYRQMLLDTNNSQLFSYDEWREEHGDSIELVTDDHQRENPLQQLLDSNLRQRVMEAIETLPEREKLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL | bacterial-type flagellum assembly bacterial-type flagellum-dependent cell motility DNA-templated transcription initiation regulation of DNA-templated transcription regulation of DNA-templated transcription initiation cytosol; cytosolic DNA-directed RNA polymerase complex DNA binding DNA-directed 5'-3' RNA polymerase activity sigma factor activity Escherichia coli 3D-structure Cytoplasm DNA-binding Reference proteome Sigma factor Transcription Transcription regulation MNSLYTAEGV MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVERYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAIGQLEQELGRNATETEVAERLGIDIADYRQMLLDTNNSQLFSYDEWREEHGDSIELVTDDHQRENPLQQLLDSNLRQRVMEAIETLPEREKLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL |
cysteine transmembrane transport L-cystine transport sulfur utilization | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; outer membrane-bounded periplasmic space | amino acid binding L-cystine transmembrane transporter activity ligand-gated monoatomic ion channel activity | Escherichia coli | Amino-acid transport Direct protein sequencing Periplasm Reference proteome Signal Transport | MKLAHLGRQA | MKLAHLGRQALMGVMAVALVAGMSVKSFADEGLLNKVKERGTLLVGLEGTYPPFSFQGDDGKLTGFEVEFAQQLAKHLGVEASLKPTKWDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTISGIQALVKKGNEGTIKTADDLKGKKVGVGLGTNYEEWLRQNVQGVDVRTYDDDPTKYQDLRVGRIDAILVDRLAALDLVKKTNDTLAVTGEAFSRQESGVALRKGNEDLLKAVNDAIAEMQKDGTLQALSEKWFGADVTK | cysteine transmembrane transport L-cystine transport sulfur utilization ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; outer membrane-bounded periplasmic space amino acid binding L-cystine transmembrane transporter activity ligand-gated monoatomic ion channel activity Escherichia coli Amino-acid transport Direct protein sequencing Periplasm Reference proteome Signal Transport MKLAHLGRQA MKLAHLGRQALMGVMAVALVAGMSVKSFADEGLLNKVKERGTLLVGLEGTYPPFSFQGDDGKLTGFEVEFAQQLAKHLGVEASLKPTKWDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTISGIQALVKKGNEGTIKTADDLKGKKVGVGLGTNYEEWLRQNVQGVDVRTYDDDPTKYQDLRVGRIDAILVDRLAALDLVKKTNDTLAVTGEAFSRQESGVALRKGNEDLLKAVNDAIAEMQKDGTLQALSEKWFGADVTK |
iron ion transport protein repair response to oxidative stress | cytosol | enzyme activator activity riboflavin reductase (NAD(P)H) activity riboflavin reductase (NADPH) activity | Escherichia coli | 3D-structure Direct protein sequencing FAD Flavoprotein FMN Ion transport Iron Iron transport NAD NADP Oxidoreductase Reference proteome Transport | MTTLSCKVTS | MTTLSCKVTSVEAITDTVYRVRIVPDAAFSFRAGQYLMVVMDERDKRPFSMASTPDEKGFIELHIGASEINLYAKAVMDRILKDHQIVVDIPHGEAWLRDDEERPMILIAGGTGFSYARSILLTALARNPNRDITIYWGGREEQHLYDLCELEALSLKHPGLQVVPVVEQPEAGWRGRTGTVLTAVLQDHGTLAEHDIYIAGRFEMAKIARDLFCSERNAREDRLFGDAFAFI | iron ion transport protein repair response to oxidative stress cytosol enzyme activator activity riboflavin reductase (NAD(P)H) activity riboflavin reductase (NADPH) activity Escherichia coli 3D-structure Direct protein sequencing FAD Flavoprotein FMN Ion transport Iron Iron transport NAD NADP Oxidoreductase Reference proteome Transport MTTLSCKVTS MTTLSCKVTSVEAITDTVYRVRIVPDAAFSFRAGQYLMVVMDERDKRPFSMASTPDEKGFIELHIGASEINLYAKAVMDRILKDHQIVVDIPHGEAWLRDDEERPMILIAGGTGFSYARSILLTALARNPNRDITIYWGGREEQHLYDLCELEALSLKHPGLQVVPVVEQPEAGWRGRTGTVLTAVLQDHGTLAEHDIYIAGRFEMAKIARDLFCSERNAREDRLFGDAFAFI |
fucose metabolic process fucosylation L-fucose metabolic process | cytoplasm | D-ribose pyranase activity fucose binding identical protein binding L-fucose mutarotase activity racemase and epimerase activity, acting on carbohydrates and derivatives | Escherichia coli | 3D-structure Carbohydrate metabolism Cytoplasm Fucose metabolism Isomerase Reference proteome | MLKTISPLIS | MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAPPLVMMAAVEGDTLDPEVERRYRNALSLQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP | fucose metabolic process fucosylation L-fucose metabolic process cytoplasm D-ribose pyranase activity fucose binding identical protein binding L-fucose mutarotase activity racemase and epimerase activity, acting on carbohydrates and derivatives Escherichia coli 3D-structure Carbohydrate metabolism Cytoplasm Fucose metabolism Isomerase Reference proteome MLKTISPLIS MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAPPLVMMAAVEGDTLDPEVERRYRNALSLQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP |
colanic acid biosynthetic process galactose catabolic process via UDP-galactose lipopolysaccharide core region biosynthetic process osmoregulated periplasmic glucan biosynthetic process UDP-glucose metabolic process | cytosol; protein-containing complex | identical protein binding magnesium ion binding UTP:glucose-1-phosphate uridylyltransferase activity | Escherichia coli | 3D-structure Direct protein sequencing Magnesium Nucleotidyltransferase Reference proteome Transferase | MAAINTKVKK | MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK | colanic acid biosynthetic process galactose catabolic process via UDP-galactose lipopolysaccharide core region biosynthetic process osmoregulated periplasmic glucan biosynthetic process UDP-glucose metabolic process cytosol; protein-containing complex identical protein binding magnesium ion binding UTP:glucose-1-phosphate uridylyltransferase activity Escherichia coli 3D-structure Direct protein sequencing Magnesium Nucleotidyltransferase Reference proteome Transferase MAAINTKVKK MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK |
glycolate catabolic process glyoxylate catabolic process isoleucine biosynthetic process valine biosynthetic process | acetolactate synthase complex | FAD binding flavin adenine dinucleotide binding identical protein binding magnesium ion binding tartronate-semialdehyde synthase activity thiamine pyrophosphate binding | Escherichia coli | 3D-structure Direct protein sequencing Lyase Magnesium Reference proteome Thiamine pyrophosphate | MAKMRAVDAA | MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHIDIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWVADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE | glycolate catabolic process glyoxylate catabolic process isoleucine biosynthetic process valine biosynthetic process acetolactate synthase complex FAD binding flavin adenine dinucleotide binding identical protein binding magnesium ion binding tartronate-semialdehyde synthase activity thiamine pyrophosphate binding Escherichia coli 3D-structure Direct protein sequencing Lyase Magnesium Reference proteome Thiamine pyrophosphate MAKMRAVDAA MAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELMAGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHIDIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWVADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDFQFLIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVVEVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE |
DNA damage response glycolate catabolic process | glycolate oxidase complex; plasma membrane | (S)-2-hydroxy-acid oxidase activity D-2-hydroxy-acid dehydrogenase activity FAD binding glycolate dehydrogenase activity | Escherichia coli | Cell inner membrane Cell membrane FAD Flavoprotein Membrane Oxidoreductase Reference proteome | MSILYEERLD | MSILYEERLDGALPDVDRTSVLMALREHVPGLEILHTDEEIIPYECDGLSAYRTRPLLVVLPKQMEQVTAILAVCHRLRVPVVTRGAGTGLSGGALPLEKGVLLVMARFKEILDINPVGRRARVQPGVRNLAISQAVAPHNLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKIEVQTLDGEALTLGSDALDSPGFDLLALFTGSEGMLGVTTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIANGIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCMDGTIPRRALPGVLEGIARLSQQYDLRVANVFHAGDGNMHPLILFDANEPGEFARAEELGGKILELCVEVGGSISGEHGIGREKINQMCAQFNSDEITTFHAVKAAFDPDGLLNPGKNIPTLHRCAEFGAMHVHHGHLPFPELERF | DNA damage response glycolate catabolic process glycolate oxidase complex; plasma membrane (S)-2-hydroxy-acid oxidase activity D-2-hydroxy-acid dehydrogenase activity FAD binding glycolate dehydrogenase activity Escherichia coli Cell inner membrane Cell membrane FAD Flavoprotein Membrane Oxidoreductase Reference proteome MSILYEERLD MSILYEERLDGALPDVDRTSVLMALREHVPGLEILHTDEEIIPYECDGLSAYRTRPLLVVLPKQMEQVTAILAVCHRLRVPVVTRGAGTGLSGGALPLEKGVLLVMARFKEILDINPVGRRARVQPGVRNLAISQAVAPHNLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKIEVQTLDGEALTLGSDALDSPGFDLLALFTGSEGMLGVTTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIANGIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCMDGTIPRRALPGVLEGIARLSQQYDLRVANVFHAGDGNMHPLILFDANEPGEFARAEELGGKILELCVEVGGSISGEHGIGREKINQMCAQFNSDEITTFHAVKAAFDPDGLLNPGKNIPTLHRCAEFGAMHVHHGHLPFPELERF |
cellular response to mercury ion glycerol transmembrane transport | plasma membrane | glycerol channel activity glycerol transmembrane transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport | MSQTSTLKGQ | MSQTSTLKGQCIAEFLGTGLLIFFGVGCVAALKVAGASFGQWEISVIWGLGVAMAIYLTAGVSGAHLNPAVTIALWLFACFDKRKVIPFIVSQVAGAFCAAALVYGLYYNLFFDFEQTHHIVRGSVESVDLAGTFSTYPNPHINFVQAFAVEMVITAILMGLILALTDDGNGVPRGPLAPLLIGLLIAVIGASMGPLTGFAMNPARDFGPKVFAWLAGWGNVAFTGGRDIPYFLVPLFGPIVGAIVGAFAYRKLIGRHLPCDICVVEEKETTTPSEQKASL | cellular response to mercury ion glycerol transmembrane transport plasma membrane glycerol channel activity glycerol transmembrane transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport MSQTSTLKGQ MSQTSTLKGQCIAEFLGTGLLIFFGVGCVAALKVAGASFGQWEISVIWGLGVAMAIYLTAGVSGAHLNPAVTIALWLFACFDKRKVIPFIVSQVAGAFCAAALVYGLYYNLFFDFEQTHHIVRGSVESVDLAGTFSTYPNPHINFVQAFAVEMVITAILMGLILALTDDGNGVPRGPLAPLLIGLLIAVIGASMGPLTGFAMNPARDFGPKVFAWLAGWGNVAFTGGRDIPYFLVPLFGPIVGAIVGAFAYRKLIGRHLPCDICVVEEKETTTPSEQKASL |
glutathione metabolic process spermidine metabolic process | cytosol | ATP binding glutathionylspermidine amidase activity glutathionylspermidine synthase activity metal ion binding | Escherichia coli | 3D-structure ATP-binding Direct protein sequencing Hydrolase Ligase Magnesium Metal-binding Multifunctional enzyme Nucleotide-binding Oxidation Reference proteome | MSKGTTSQDA | MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWAEQGYKGNGFNPAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMEQALHQAGFETRILRGLDELGWDAAGQLIDGEGRLVNCVWKTWAWETAFDQIREVSDREFAAVPIRTGHPQNEVRLIDVLLRPEVLVFEPLWTVIPGNKAILPILWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCGSNIDLVSHHEEVLDKTSGKFAEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDESLVIKKESDIEPLIVVKK | glutathione metabolic process spermidine metabolic process cytosol ATP binding glutathionylspermidine amidase activity glutathionylspermidine synthase activity metal ion binding Escherichia coli 3D-structure ATP-binding Direct protein sequencing Hydrolase Ligase Magnesium Metal-binding Multifunctional enzyme Nucleotide-binding Oxidation Reference proteome MSKGTTSQDA MSKGTTSQDAPFGTLLGYAPGGVAIYSSDYSSLDPQEYEDDAVFRSYIDDEYMGHKWQCVEFARRFLFLNYGVVFTDVGMAWEIFSLRFLREVVNDNILPLQAFPNGSPRAPVAGALLIWDKGGEFKDTGHVAIITQLHGNKVRIAEQNVIHSPLPQGQQWTRELEMVVENGCYTLKDTFDDTTILGWMIQTEDTEYSLPQPEIAGELLKISGARLENKGQFDGKWLDEKDPLQNAYVQANGQVINQDPYHYYTITESAEQELIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWQRRRHHMITGRMDFCMDERGLKVYEYNADSASCHTEAGLILERWAEQGYKGNGFNPAEGLINELAGAWKHSRARPFVHIMQDKDIEENYHAQFMEQALHQAGFETRILRGLDELGWDAAGQLIDGEGRLVNCVWKTWAWETAFDQIREVSDREFAAVPIRTGHPQNEVRLIDVLLRPEVLVFEPLWTVIPGNKAILPILWSLFPHHRYLLDTDFTVNDELVKTGYAVKPIAGRCGSNIDLVSHHEEVLDKTSGKFAEQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDESLVIKKESDIEPLIVVKK |
DNA topological change DNA-templated DNA replication DNA-templated transcription negative regulation of DNA-templated DNA replication response to antibiotic response to xenobiotic stimulus | chromosome; cytoplasm; cytosol; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; membrane | ATP binding ATP-dependent activity, acting on DNA DNA binding DNA negative supercoiling activity DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity identical protein binding | Escherichia coli | 3D-structure Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing DNA-binding Isomerase Nucleotide-binding Reference proteome Topoisomerase | MSDLAREITP | MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNVAAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVVVTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVYSMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVLTEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTGVRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERNGLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVAEPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE | DNA topological change DNA-templated DNA replication DNA-templated transcription negative regulation of DNA-templated DNA replication response to antibiotic response to xenobiotic stimulus chromosome; cytoplasm; cytosol; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; membrane ATP binding ATP-dependent activity, acting on DNA DNA binding DNA negative supercoiling activity DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity identical protein binding Escherichia coli 3D-structure Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing DNA-binding Isomerase Nucleotide-binding Reference proteome Topoisomerase MSDLAREITP MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNVAAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVVVTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVYSMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVLTEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTGVRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERNGLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVAEPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE |
DNA topological change DNA-templated DNA replication DNA-templated transcription response to antibiotic response to xenobiotic stimulus | chromosome; cytoplasm; cytosol; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex | ATP binding ATP-dependent activity, acting on DNA DNA binding DNA negative supercoiling activity DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity metal ion binding | Escherichia coli | 3D-structure Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing DNA-binding Isomerase Magnesium Metal-binding Nucleotide-binding Potassium Reference proteome Sodium Topoisomerase | MSNSYDSSSI | MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI | DNA topological change DNA-templated DNA replication DNA-templated transcription response to antibiotic response to xenobiotic stimulus chromosome; cytoplasm; cytosol; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex ATP binding ATP-dependent activity, acting on DNA DNA binding DNA negative supercoiling activity DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity metal ion binding Escherichia coli 3D-structure Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing DNA-binding Isomerase Magnesium Metal-binding Nucleotide-binding Potassium Reference proteome Sodium Topoisomerase MSNSYDSSSI MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI |
cellular stress response to acidic pH chaperone-mediated protein folding | outer membrane-bounded periplasmic space | identical protein binding protein folding chaperone protein homodimerization activity unfolded protein binding | Escherichia coli | 3D-structure Chaperone Direct protein sequencing Disulfide bond Periplasm Reference proteome Signal | MKKVLGVILG | MKKVLGVILGGLLLLPVVSNAADAQKAADNKKPVNSWTCEDFLAVDESFQPTAVGFAEALNNKDKPEDAVLDVQGIATVTPAIVQACTQDKQANFKDKVKGEWDKIKKDM | cellular stress response to acidic pH chaperone-mediated protein folding outer membrane-bounded periplasmic space identical protein binding protein folding chaperone protein homodimerization activity unfolded protein binding Escherichia coli 3D-structure Chaperone Direct protein sequencing Disulfide bond Periplasm Reference proteome Signal MKKVLGVILG MKKVLGVILGGLLLLPVVSNAADAQKAADNKKPVNSWTCEDFLAVDESFQPTAVGFAEALNNKDKPEDAVLDVQGIATVTPAIVQACTQDKQANFKDKVKGEWDKIKKDM |
cellular stress response to acidic pH response to acidic pH | outer membrane-bounded periplasmic space | unfolded protein binding | Escherichia coli | 3D-structure Acetylation Chaperone Direct protein sequencing Periplasm Reference proteome Signal | MNISSLRKAF | MNISSLRKAFIFMGAVAALSLVNAQSALAANESAKDMTCQEFIDLNPKAMTPVAWWMLHEETVYKGGDTVTLNETDLTQIPKVIEYCKKNPQKNLYTFKNQASNDLPN | cellular stress response to acidic pH response to acidic pH outer membrane-bounded periplasmic space unfolded protein binding Escherichia coli 3D-structure Acetylation Chaperone Direct protein sequencing Periplasm Reference proteome Signal MNISSLRKAF MNISSLRKAFIFMGAVAALSLVNAQSALAANESAKDMTCQEFIDLNPKAMTPVAWWMLHEETVYKGGDTVTLNETDLTQIPKVIEYCKKNPQKNLYTFKNQASNDLPN |
bile acid catabolic process lipid catabolic process | cytosol; protein-containing complex | chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity cholate 7-alpha-dehydrogenase activity identical protein binding NAD binding | Escherichia coli | 3D-structure Bile acid catabolism Direct protein sequencing Lipid degradation Lipid metabolism NAD Oxidoreductase Reference proteome Steroid metabolism | MFNSDNLRLD | MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN | bile acid catabolic process lipid catabolic process cytosol; protein-containing complex chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity cholate 7-alpha-dehydrogenase activity identical protein binding NAD binding Escherichia coli 3D-structure Bile acid catabolism Direct protein sequencing Lipid degradation Lipid metabolism NAD Oxidoreductase Reference proteome Steroid metabolism MFNSDNLRLD MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN |
chaperone-mediated protein folding Gram-negative-bacterium-type cell outer membrane assembly protein folding protein insertion into membrane from inner side protein maturation by protein folding protein stabilization | cytosol; outer membrane-bounded periplasmic space | identical protein binding lipopolysaccharide binding unfolded protein binding | Escherichia coli | 3D-structure Chaperone Direct protein sequencing Periplasm Reference proteome Signal | MKKWLLAAGL | MKKWLLAAGLGLALATSAQAADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK | chaperone-mediated protein folding Gram-negative-bacterium-type cell outer membrane assembly protein folding protein insertion into membrane from inner side protein maturation by protein folding protein stabilization cytosol; outer membrane-bounded periplasmic space identical protein binding lipopolysaccharide binding unfolded protein binding Escherichia coli 3D-structure Chaperone Direct protein sequencing Periplasm Reference proteome Signal MKKWLLAAGL MKKWLLAAGLGLALATSAQAADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK |
negative regulation of DNA-templated transcription positive regulation of proteolysis protein destabilization regulation of DNA-templated transcription | cytosol; protein-DNA complex; sigma factor antagonist complex | phosphorelay response regulator activity sigma factor antagonist activity transcription cis-regulatory region binding | Escherichia coli | 3D-structure Phosphoprotein Reference proteome Stress response | MTQPLVGKQI | MTQPLVGKQILIVEDEQVFRSLLDSWFSSLGATTVLAADGVDALELLGGFTPDLMICDIAMPRMNGLKLLEHIRNRGDQTPVLVISATENMADIAKALRLGVEDVLLKPVKDLNRLREMVFACLYPSMFNSRVEEEERLFRDWDAMVDNPAAAAKLLQELQPPVQQVISHCRVNYRQLVAADKPGLVLDIAALSENDLAFYCLDVTRAGHNGVLAALLLRALFNGLLQEQLAHQNQRLPELGALLKQVNHLLRQANLPGQFPLLVGYYHRELKNLILVSAGLNATLNTGEHQVQISNGVPLGTLGNAYLNQLSQRCDAWQCQIWGTGGRLRLMLSAE | negative regulation of DNA-templated transcription positive regulation of proteolysis protein destabilization regulation of DNA-templated transcription cytosol; protein-DNA complex; sigma factor antagonist complex phosphorelay response regulator activity sigma factor antagonist activity transcription cis-regulatory region binding Escherichia coli 3D-structure Phosphoprotein Reference proteome Stress response MTQPLVGKQI MTQPLVGKQILIVEDEQVFRSLLDSWFSSLGATTVLAADGVDALELLGGFTPDLMICDIAMPRMNGLKLLEHIRNRGDQTPVLVISATENMADIAKALRLGVEDVLLKPVKDLNRLREMVFACLYPSMFNSRVEEEERLFRDWDAMVDNPAAAAKLLQELQPPVQQVISHCRVNYRQLVAADKPGLVLDIAALSENDLAFYCLDVTRAGHNGVLAALLLRALFNGLLQEQLAHQNQRLPELGALLKQVNHLLRQANLPGQFPLLVGYYHRELKNLILVSAGLNATLNTGEHQVQISNGVPLGTLGNAYLNQLSQRCDAWQCQIWGTGGRLRLMLSAE |
fructose catabolic process | cytosol | 1-phosphofructokinase activity ATP binding phosphofructokinase activity | Escherichia coli | ATP-binding Kinase Magnesium Nucleotide-binding Reference proteome Transferase | MSRRVATITL | MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPEMKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSVDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRPQLAAMMARVDLQPFN | fructose catabolic process cytosol 1-phosphofructokinase activity ATP binding phosphofructokinase activity Escherichia coli ATP-binding Kinase Magnesium Nucleotide-binding Reference proteome Transferase MSRRVATITL MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPEMKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSVDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRPQLAAMMARVDLQPFN |
branched-chain amino acid transport D-alanine transport isoleucine transmembrane transport L-alanine transport L-isoleucine import across plasma membrane L-valine transmembrane transport leucine import across plasma membrane phenylalanine transport | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; membrane; plasma membrane | branched-chain amino acid transmembrane transporter activity L-isoleucine transmembrane transporter activity L-leucine transmembrane transporter activity L-phenylalanine transmembrane transporter activity L-valine transmembrane transporter activity | Escherichia coli | Amino-acid transport Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport | MSEQFLYFLQ | MSEQFLYFLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTGWLLVAAGFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSIFLQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSASITTMQAVIWIVTFLAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTAAVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYKDVVSFALLILVLLVMPTGILGRPEVEKV | branched-chain amino acid transport D-alanine transport isoleucine transmembrane transport L-alanine transport L-isoleucine import across plasma membrane L-valine transmembrane transport leucine import across plasma membrane phenylalanine transport ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; membrane; plasma membrane branched-chain amino acid transmembrane transporter activity L-isoleucine transmembrane transporter activity L-leucine transmembrane transporter activity L-phenylalanine transmembrane transporter activity L-valine transmembrane transporter activity Escherichia coli Amino-acid transport Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport MSEQFLYFLQ MSEQFLYFLQQMFNGVTLGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYVSFMIIAALMMMGIDTGWLLVAAGFVGAIVIASAYGWSIERVAYRPVRNSKRLIALISAIGMSIFLQNYVSLTEGSRDVALPSLFNGQWVVGHSENFSASITTMQAVIWIVTFLAMLALTIFIRYSRMGRACRACAEDLKMASLLGINTDRVIALTFVIGAAMAAVAGVLLGQFYGVINPYIGFMAGMKAFTAAVLGGIGSIPGAMIGGLILGIAEALSSAYLSTEYKDVVSFALLILVLLVMPTGILGRPEVEKV |
carbohydrate transport cell chemotaxis detection of maltose stimulus DNA damage response maltodextrin transmembrane transport maltose transport | ATP-binding cassette (ABC) transporter complex; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; maltose transport complex; membrane; outer membrane-bounded periplasmic space; periplasmic space | carbohydrate transmembrane transporter activity maltose binding | Escherichia coli | 3D-structure Direct protein sequencing Periplasm Reference proteome Signal Sugar transport Transport | MKIKTGARIL | MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK | carbohydrate transport cell chemotaxis detection of maltose stimulus DNA damage response maltodextrin transmembrane transport maltose transport ATP-binding cassette (ABC) transporter complex; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; maltose transport complex; membrane; outer membrane-bounded periplasmic space; periplasmic space carbohydrate transmembrane transporter activity maltose binding Escherichia coli 3D-structure Direct protein sequencing Periplasm Reference proteome Signal Sugar transport Transport MKIKTGARIL MKIKTGARILALSALTTMMFSASALAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK |
regulation of cellular pH response to antibiotic xenobiotic detoxification by transmembrane export across the plasma membrane | plasma membrane | potassium:proton antiporter activity sodium:proton antiporter activity | Escherichia coli | 3D-structure Antibiotic resistance Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport | MQNKLASGAR | MQNKLASGARLGRQALLFPLCLVLYEFSTYIGNDMIQPGMLAVVEQYQAGIDWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLAGVVWFIVTCLAILLAQNIEQFTLLRFLQGISLCFIGAVGYAAIQESFEEAVCIKITALMANVALIAPLLGPLVGAAWIHVLPWEGMFVLFAALAAISFFGLQRAMPETATRIGEKLSLKELGRDYKLVLKNGRFVAGALALGFVSLPLLAWIAQSPIIIITGEQLSSYEYGLLQVPIFGALIAGNLLLARLTSRRTVRSLIIMGGWPIMIGLLVAAAATVISSHAYLWMTAGLSIYAFGIGLANAGLVRLTLFASDMSKGTVSAAMGMLQMLIFTVGIEISKHAWLNGGNGLFNLFNLVNGILWLSLMVIFLKDKQMGNSHEG | regulation of cellular pH response to antibiotic xenobiotic detoxification by transmembrane export across the plasma membrane plasma membrane potassium:proton antiporter activity sodium:proton antiporter activity Escherichia coli 3D-structure Antibiotic resistance Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport MQNKLASGAR MQNKLASGARLGRQALLFPLCLVLYEFSTYIGNDMIQPGMLAVVEQYQAGIDWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLAGVVWFIVTCLAILLAQNIEQFTLLRFLQGISLCFIGAVGYAAIQESFEEAVCIKITALMANVALIAPLLGPLVGAAWIHVLPWEGMFVLFAALAAISFFGLQRAMPETATRIGEKLSLKELGRDYKLVLKNGRFVAGALALGFVSLPLLAWIAQSPIIIITGEQLSSYEYGLLQVPIFGALIAGNLLLARLTSRRTVRSLIIMGGWPIMIGLLVAAAATVISSHAYLWMTAGLSIYAFGIGLANAGLVRLTLFASDMSKGTVSAAMGMLQMLIFTVGIEISKHAWLNGGNGLFNLFNLVNGILWLSLMVIFLKDKQMGNSHEG |
methionine biosynthetic process tetrahydrofolate interconversion | cytosol; protein-containing complex | FAD binding methylenetetrahydrofolate reductase (NAD(P)H) activity methylenetetrahydrofolate reductase NADH activity protein-folding chaperone binding | Escherichia coli | 3D-structure Amino-acid biosynthesis FAD Flavoprotein Methionine biosynthesis NAD Oxidoreductase Reference proteome | MSFFHASQRD | MSFFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPGL | methionine biosynthetic process tetrahydrofolate interconversion cytosol; protein-containing complex FAD binding methylenetetrahydrofolate reductase (NAD(P)H) activity methylenetetrahydrofolate reductase NADH activity protein-folding chaperone binding Escherichia coli 3D-structure Amino-acid biosynthesis FAD Flavoprotein Methionine biosynthesis NAD Oxidoreductase Reference proteome MSFFHASQRD MSFFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPGL |
cell division chromosome segregation division septum assembly negative regulation of cell division | cell pole; cytoplasmic side of plasma membrane; cytosol; plasma membrane | ATP binding ATP hydrolysis activity identical protein binding | Escherichia coli | 3D-structure ATP-binding Cell cycle Cell division Cell inner membrane Cell membrane Direct protein sequencing Membrane Nucleotide-binding Reference proteome Septation | MARIIVVTSG | MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG | cell division chromosome segregation division septum assembly negative regulation of cell division cell pole; cytoplasmic side of plasma membrane; cytosol; plasma membrane ATP binding ATP hydrolysis activity identical protein binding Escherichia coli 3D-structure ATP-binding Cell cycle Cell division Cell inner membrane Cell membrane Direct protein sequencing Membrane Nucleotide-binding Reference proteome Septation MARIIVVTSG MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG |
bacterial-type flagellum-dependent cell motility chemotaxis proton transmembrane transport | bacterial-type flagellum; bacterial-type flagellum stator complex; plasma membrane | proton channel activity | Escherichia coli | Cell inner membrane Cell membrane Chemotaxis Flagellar rotation Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix | MKNQAHPIIV | MKNQAHPIIVVKRRKAKSHGAAHGSWKIAYADFMTAMMAFFLVMWLISISSPKELIQIAEYFRTPLATAVTGGDRISNSESPIPGGGDDYTQSQGEVNKQPNIEELKKRMEQSRLRKLRGDLDQLIESDPKLRALRPHLKIDLVQEGLRIQIIDSQNRPMFRTGSADVEPYMRDILRAIAPVLNGIPNRISLSGHTDDFPYASGEKGYSNWELSADRANASRRELMVGGLDSGKVLRVVGMAATMRLSDRGPDDAVNRRISLLVLNKQAEQAILHENAESQNEPVSALEKPEVAPQVSVPTMPSAEPR | bacterial-type flagellum-dependent cell motility chemotaxis proton transmembrane transport bacterial-type flagellum; bacterial-type flagellum stator complex; plasma membrane proton channel activity Escherichia coli Cell inner membrane Cell membrane Chemotaxis Flagellar rotation Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix MKNQAHPIIV MKNQAHPIIVVKRRKAKSHGAAHGSWKIAYADFMTAMMAFFLVMWLISISSPKELIQIAEYFRTPLATAVTGGDRISNSESPIPGGGDDYTQSQGEVNKQPNIEELKKRMEQSRLRKLRGDLDQLIESDPKLRALRPHLKIDLVQEGLRIQIIDSQNRPMFRTGSADVEPYMRDILRAIAPVLNGIPNRISLSGHTDDFPYASGEKGYSNWELSADRANASRRELMVGGLDSGKVLRVVGMAATMRLSDRGPDDAVNRRISLLVLNKQAEQAILHENAESQNEPVSALEKPEVAPQVSVPTMPSAEPR |
L-methionine salvage from methylthioadenosine L-methionine salvage from S-adenosylmethionine purine deoxyribonucleoside catabolic process toxic metabolite repair | cytosol | adenosylhomocysteine nucleosidase activity identical protein binding methylthioadenosine nucleosidase activity protein homodimerization activity | Escherichia coli | 3D-structure Amino-acid biosynthesis Hydrolase Methionine biosynthesis Reference proteome | MKIGIIGAME | MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG | L-methionine salvage from methylthioadenosine L-methionine salvage from S-adenosylmethionine purine deoxyribonucleoside catabolic process toxic metabolite repair cytosol adenosylhomocysteine nucleosidase activity identical protein binding methylthioadenosine nucleosidase activity protein homodimerization activity Escherichia coli 3D-structure Amino-acid biosynthesis Hydrolase Methionine biosynthesis Reference proteome MKIGIIGAME MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG |
cell wall organization glycolipid translocation lipid translocation lipid-linked peptidoglycan transport peptidoglycan biosynthetic process regulation of cell shape | division septum; plasma membrane | cardiolipin binding lipid-linked peptidoglycan transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Cell shape Cell wall biogenesis/degradation Membrane Peptidoglycan synthesis Reference proteome Transmembrane Transmembrane helix Transport | MNLLKSLAAV | MNLLKSLAAVSSMTMFSRVLGFARDAIVARIFGAGMATDAFFVAFKLPNLLRRIFAEGAFSQAFVPILAEYKSKQGEDATRVFVSYVSGLLTLALAVVTVAGMLAAPWVIMVTAPGFADTADKFALTSQLLKITFPYILLISLASLVGAILNTWNRFSIPAFAPTLLNISMIGFALFAAPYFNPPVLALAWAVTVGGVLQLVYQLPHLKKIGMLVLPRINFHDAGAMRVVKQMGPAILGVSVSQISLIINTIFASFLASGSVSWMYYADRLMEFPSGVLGVALGTILLPSLSKSFASGNHDEYNRLMDWGLRLCFLLALPSAVALGILSGPLTVSLFQYGKFTAFDALMTQRALIAYSVGLIGLIVVKVLAPGFYSRQDIKTPVKIAIVTLILTQLMNLAFIGPLKHAGLSLSIGLAACLNASLLYWQLRKQKIFTPQPGWMAFLLRLVVAVLVMSGVLLGMLHIMPEWSLGTMPWRLLRLMAVVLAGIAAYFAALAVLGFKVKEFARRTV | cell wall organization glycolipid translocation lipid translocation lipid-linked peptidoglycan transport peptidoglycan biosynthetic process regulation of cell shape division septum; plasma membrane cardiolipin binding lipid-linked peptidoglycan transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Cell shape Cell wall biogenesis/degradation Membrane Peptidoglycan synthesis Reference proteome Transmembrane Transmembrane helix Transport MNLLKSLAAV MNLLKSLAAVSSMTMFSRVLGFARDAIVARIFGAGMATDAFFVAFKLPNLLRRIFAEGAFSQAFVPILAEYKSKQGEDATRVFVSYVSGLLTLALAVVTVAGMLAAPWVIMVTAPGFADTADKFALTSQLLKITFPYILLISLASLVGAILNTWNRFSIPAFAPTLLNISMIGFALFAAPYFNPPVLALAWAVTVGGVLQLVYQLPHLKKIGMLVLPRINFHDAGAMRVVKQMGPAILGVSVSQISLIINTIFASFLASGSVSWMYYADRLMEFPSGVLGVALGTILLPSLSKSFASGNHDEYNRLMDWGLRLCFLLALPSAVALGILSGPLTVSLFQYGKFTAFDALMTQRALIAYSVGLIGLIVVKVLAPGFYSRQDIKTPVKIAIVTLILTQLMNLAFIGPLKHAGLSLSIGLAACLNASLLYWQLRKQKIFTPQPGWMAFLLRLVVAVLVMSGVLLGMLHIMPEWSLGTMPWRLLRLMAVVLAGIAAYFAALAVLGFKVKEFARRTV |
carbohydrate metabolic process N-acetylglucosamine catabolic process N-acetylneuraminate catabolic process protein homotetramerization | protein-containing complex | identical protein binding N-acetylgalactosamine-6-phosphate deacetylase activity N-acetylglucosamine-6-phosphate deacetylase activity zinc ion binding | Escherichia coli | 3D-structure Carbohydrate metabolism Hydrolase Metal-binding Reference proteome Zinc | MYALTQGRIF | MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTAFTPDFKITKTIVNGNEVVTQ | carbohydrate metabolic process N-acetylglucosamine catabolic process N-acetylneuraminate catabolic process protein homotetramerization protein-containing complex identical protein binding N-acetylgalactosamine-6-phosphate deacetylase activity N-acetylglucosamine-6-phosphate deacetylase activity zinc ion binding Escherichia coli 3D-structure Carbohydrate metabolism Hydrolase Metal-binding Reference proteome Zinc MYALTQGRIF MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTAFTPDFKITKTIVNGNEVVTQ |
carbohydrate metabolic process UMP catabolic process | cytosol | 5'-nucleotidase activity magnesium ion binding phosphatase activity XMP 5'-nucleosidase activity | Escherichia coli | 3D-structure Carbohydrate metabolism Hydrolase Magnesium Metal-binding Reference proteome | MTIKNVICDI | MTIKNVICDIDGVLMHDNVAVPGAAEFLHGIMDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQEGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSSLDDIDSMPFRPSWIYPSVAEIDVI | carbohydrate metabolic process UMP catabolic process cytosol 5'-nucleotidase activity magnesium ion binding phosphatase activity XMP 5'-nucleosidase activity Escherichia coli 3D-structure Carbohydrate metabolism Hydrolase Magnesium Metal-binding Reference proteome MTIKNVICDI MTIKNVICDIDGVLMHDNVAVPGAAEFLHGIMDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQEGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSSLDDIDSMPFRPSWIYPSVAEIDVI |
nitrate assimilation phosphorelay signal transduction system regulation of DNA-templated transcription | cytosol; protein-DNA complex | ATP binding DNA binding DNA-binding transcription repressor activity identical protein binding transcription cis-regulatory region binding | Escherichia coli | 3D-structure Activator ATP-binding DNA-binding Nitrate assimilation Nucleotide-binding Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Two-component regulatory system | MSNQEPATIL | MSNQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALHQAAAGEMVLSEALTPVLAASLRANRATTERDVNQLTPRERDILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERIF | nitrate assimilation phosphorelay signal transduction system regulation of DNA-templated transcription cytosol; protein-DNA complex ATP binding DNA binding DNA-binding transcription repressor activity identical protein binding transcription cis-regulatory region binding Escherichia coli 3D-structure Activator ATP-binding DNA-binding Nitrate assimilation Nucleotide-binding Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Two-component regulatory system MSNQEPATIL MSNQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALHQAAAGEMVLSEALTPVLAASLRANRATTERDVNQLTPRERDILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERIF |
anaerobic electron transport chain anaerobic respiration nitrate assimilation nitrate metabolic process | membrane; nitrate reductase complex; plasma membrane | electron transfer activity heme binding metal ion binding nitrate reductase activity | Escherichia coli | Cell inner membrane Cell membrane Electron transport Heme Iron Membrane Metal-binding Nitrate assimilation Oxidoreductase Reference proteome Transmembrane Transmembrane helix Transport | MIQYLNVFFY | MIQYLNVFFYDIYPYICATVFFLGSWLRYDYGQYTWRASSSQMLDKRGMVIWSNLFHIGILGIFFGHLFGMLTPHWMYAWFLPVAAKQLMAMVLGGICGVLTLIGGAGLLWRRLTNQRVRATSTTPDIIIMSILLIQCLLGLSTIPFSAQYPDGSEMMKLVGWAQSIVTFRGGSSEMLNGVAFVFRLHLVLGMTIFLLFPFTRLVHVWSAPFEYFTRRYQIVRSRR | anaerobic electron transport chain anaerobic respiration nitrate assimilation nitrate metabolic process membrane; nitrate reductase complex; plasma membrane electron transfer activity heme binding metal ion binding nitrate reductase activity Escherichia coli Cell inner membrane Cell membrane Electron transport Heme Iron Membrane Metal-binding Nitrate assimilation Oxidoreductase Reference proteome Transmembrane Transmembrane helix Transport MIQYLNVFFY MIQYLNVFFYDIYPYICATVFFLGSWLRYDYGQYTWRASSSQMLDKRGMVIWSNLFHIGILGIFFGHLFGMLTPHWMYAWFLPVAAKQLMAMVLGGICGVLTLIGGAGLLWRRLTNQRVRATSTTPDIIIMSILLIQCLLGLSTIPFSAQYPDGSEMMKLVGWAQSIVTFRGGSSEMLNGVAFVFRLHLVLGMTIFLLFPFTRLVHVWSAPFEYFTRRYQIVRSRR |
division septum assembly FtsZ-dependent cytokinesis | cell division site; cytosol | identical protein binding | Escherichia coli | 3D-structure Acetylation Cell cycle Cell division Coiled coil Cytoplasm Reference proteome Septation | MTMSLEVFEK | MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQALLGRMEEV | division septum assembly FtsZ-dependent cytokinesis cell division site; cytosol identical protein binding Escherichia coli 3D-structure Acetylation Cell cycle Cell division Coiled coil Cytoplasm Reference proteome Septation MTMSLEVFEK MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHLKEQQNGWQERLQALLGRMEEV |
guanine import across plasma membrane hypoxanthine transport | plasma membrane | guanine transmembrane transporter activity | Escherichia coli | Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport | MSTPSARTGG | MSTPSARTGGSLDAWFKISQRGSTVRQEVVAGLTTFLAMVYSVIVVPGMLGKAGFPPAAVFVATCLVAGLGSIVMGLWANLPLAIGCAISLTAFTAFSLVLGQHISVPVALGAVFLMGVLFTVISATGIRSWILRNLPHGVAHGTGIGIGLFLLLIAANGVGLVIKNPLDGLPVALGDFATFPVIMSLVGLAVIIGLEKLKVPGGILLTIIGISIVGLIFDPNVHFSGVFAMPSLSDENGNSLIGSLDIMGALNPVVLPSVLALVMTAVFDATGTIRAVAGQANLLDKDGQIIDGGKALTTDSMSSVFSGLVGAAPAAVYIESAAGTAAGGKTGLTAITVGVLFLLILFLSPLSYLVPGYATAPALMYVGLLMLSNVAKIDFADFVDAMAGLVTAVFIVLTCNIVTGIMIGFATLVIGRLVSGEWRKLNIGTVVIAVALVTFYAGGWAI | guanine import across plasma membrane hypoxanthine transport plasma membrane guanine transmembrane transporter activity Escherichia coli Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport MSTPSARTGG MSTPSARTGGSLDAWFKISQRGSTVRQEVVAGLTTFLAMVYSVIVVPGMLGKAGFPPAAVFVATCLVAGLGSIVMGLWANLPLAIGCAISLTAFTAFSLVLGQHISVPVALGAVFLMGVLFTVISATGIRSWILRNLPHGVAHGTGIGIGLFLLLIAANGVGLVIKNPLDGLPVALGDFATFPVIMSLVGLAVIIGLEKLKVPGGILLTIIGISIVGLIFDPNVHFSGVFAMPSLSDENGNSLIGSLDIMGALNPVVLPSVLALVMTAVFDATGTIRAVAGQANLLDKDGQIIDGGKALTTDSMSSVFSGLVGAAPAAVYIESAAGTAAGGKTGLTAITVGVLFLLILFLSPLSYLVPGYATAPALMYVGLLMLSNVAKIDFADFVDAMAGLVTAVFIVLTCNIVTGIMIGFATLVIGRLVSGEWRKLNIGTVVIAVALVTFYAGGWAI |
maintenance of translational fidelity tRNA threonylcarbamoyladenosine modification | cytoplasm; EKC/KEOPS complex | ADP binding ATP binding ATP hydrolysis activity identical protein binding metal ion binding protein kinase activity | Escherichia coli | ATP-binding Cytoplasm Magnesium Metal-binding Nucleotide-binding Reference proteome tRNA processing | MMNRVIPLPD | MMNRVIPLPDEQATLDLGERVAKACDGATVIYLYGDLGAGKTTFSRGFLQALGHQGNVKSPTYTLVEPYTLDNLMVYHFDLYRLADPEELEFMGIRDYFANDAICLVEWPQQGTGVLPDPDVEIHIDYQAQGREARVSAVSSAGELLLARLAG | maintenance of translational fidelity tRNA threonylcarbamoyladenosine modification cytoplasm; EKC/KEOPS complex ADP binding ATP binding ATP hydrolysis activity identical protein binding metal ion binding protein kinase activity Escherichia coli ATP-binding Cytoplasm Magnesium Metal-binding Nucleotide-binding Reference proteome tRNA processing MMNRVIPLPD MMNRVIPLPDEQATLDLGERVAKACDGATVIYLYGDLGAGKTTFSRGFLQALGHQGNVKSPTYTLVEPYTLDNLMVYHFDLYRLADPEELEFMGIRDYFANDAICLVEWPQQGTGVLPDPDVEIHIDYQAQGREARVSAVSSAGELLLARLAG |
mRNA catabolic process regulation of endoribonuclease activity | cytosol | endoribonuclease inhibitor activity enzyme binding protein homodimerization activity ribonuclease inhibitor activity | Escherichia coli | Cytoplasm Reference proteome | MANPEQLEEQ | MANPEQLEEQREETRLIIEELLEDGSDPDALYTIEHHLSADDLETLEKAAVEAFKLGYEVTDPEELEVEDGDIVICCDILSECALNADLIDAQVEQLMTLAEKFDVEYDGWGTYFEDPNGEDGDDEDFVDEDDDGVRH | mRNA catabolic process regulation of endoribonuclease activity cytosol endoribonuclease inhibitor activity enzyme binding protein homodimerization activity ribonuclease inhibitor activity Escherichia coli Cytoplasm Reference proteome MANPEQLEEQ MANPEQLEEQREETRLIIEELLEDGSDPDALYTIEHHLSADDLETLEKAAVEAFKLGYEVTDPEELEVEDGDIVICCDILSECALNADLIDAQVEQLMTLAEKFDVEYDGWGTYFEDPNGEDGDDEDFVDEDDDGVRH |
isoleucine biosynthetic process organonitrogen compound catabolic process protein homotrimerization response to toxic substance | cytosol; membrane; protein-containing complex | 2-iminobutanoate deaminase activity 2-iminopropanoate deaminase activity deaminase activity identical protein binding unfolded protein binding | Escherichia coli | 3D-structure Amino-acid biosynthesis Branched-chain amino acid biosynthesis Cytoplasm Detoxification Direct protein sequencing Hydrolase Isoleucine biosynthesis Reference proteome | MSKTIATENA | MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVRR | isoleucine biosynthetic process organonitrogen compound catabolic process protein homotrimerization response to toxic substance cytosol; membrane; protein-containing complex 2-iminobutanoate deaminase activity 2-iminopropanoate deaminase activity deaminase activity identical protein binding unfolded protein binding Escherichia coli 3D-structure Amino-acid biosynthesis Branched-chain amino acid biosynthesis Cytoplasm Detoxification Direct protein sequencing Hydrolase Isoleucine biosynthesis Reference proteome MSKTIATENA MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVRR |
cellular response to nitrate cellular response to nitrite DNA damage response nitrate assimilation signal transduction | outer membrane-bounded periplasmic space; plasma membrane | ATP binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein homodimerization activity | Escherichia coli | 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nitrate assimilation Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system | MLKRCLSPLT | MLKRCLSPLTLVNQVALIVLLSTAIGLAGMAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPALMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTFTDVQGDTHE | cellular response to nitrate cellular response to nitrite DNA damage response nitrate assimilation signal transduction outer membrane-bounded periplasmic space; plasma membrane ATP binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein homodimerization activity Escherichia coli 3D-structure ATP-binding Cell inner membrane Cell membrane Kinase Membrane Nitrate assimilation Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system MLKRCLSPLT MLKRCLSPLTLVNQVALIVLLSTAIGLAGMAVSGWLVQGVQGSAHAINKAGSLRMQSYRLLAAVPLSEKDKPLIKEMEQTAFSAELTRAAERDGQLAQLQGLQDYWRNELIPALMRAQNRETVSADVSQFVAGLDQLVSGFDRTTEMRIETVVLVHRVMAVFMALLLVFTIIWLRARLLQPWRQLLAMASAVSHRDFTQRANISGRNEMAMLGTALNNMSAELAESYAVLEQRVQEKTAGLEHKNQILSFLWQANRRLHSRAPLCERLSPVLNGLQNLTLLRDIELRVYDTDDEENHQEFTCQPDMTCDDKGCQLCPRGVLPVGDRGTTLKWRLADSHTQYGILLATLPQGRHLSHDQQQLVDTLVEQLTATLALDRHQERQQQLIVMEERATIARELHDSIAQSLSCMKMQVSCLQMQGDALPESSRELLSQIRNELNASWAQLRELLTTFRLQLTEPGLRPALEASCEEYSAKFGFPVKLDYQLPPRLVPSHQAIHLLQIAREALSNALKHSQASEVVVTVAQNDNQVKLTVQDNGCGVPENAIRSNHYGMIIMRDRAQSLRGDCRVRRRESGGTEVVVTFIPEKTFTDVQGDTHE |
response to lithium ion | plasma membrane | sodium:proton antiporter activity | Escherichia coli | Antiport Cell inner membrane Cell membrane Ion transport Membrane Reference proteome Sodium Sodium transport Transmembrane Transmembrane helix Transport | MEISWGRALW | MEISWGRALWRNFLGQSPDWYKLALIIFLIVNPLIFLISPFVAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVFIGMTSAEHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMLLSLSFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRTEDTDLQDDSHIDKHYKVVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLICGLLTCLLVEKLRWFGYGETLPEKVREVLQQFDDQSRHQRTRQDKIRLIVQAIIGVWLVTALALHLAEVGLIGLSVIILATSLTGVTDEHAIGKAFTESLPFTALLTVFFSVVAVIIDQQLFSPIIQFVLQASEHAQLSLFYIFNGLLSSISDNVFVGTIYINEAKAAMESGAITLKQYELLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTLVLTLVGLLCVEFTLAPVTEWFMQMGWIATL | response to lithium ion plasma membrane sodium:proton antiporter activity Escherichia coli Antiport Cell inner membrane Cell membrane Ion transport Membrane Reference proteome Sodium Sodium transport Transmembrane Transmembrane helix Transport MEISWGRALW MEISWGRALWRNFLGQSPDWYKLALIIFLIVNPLIFLISPFVAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVFIGMTSAEHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMLLSLSFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRTEDTDLQDDSHIDKHYKVVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLICGLLTCLLVEKLRWFGYGETLPEKVREVLQQFDDQSRHQRTRQDKIRLIVQAIIGVWLVTALALHLAEVGLIGLSVIILATSLTGVTDEHAIGKAFTESLPFTALLTVFFSVVAVIIDQQLFSPIIQFVLQASEHAQLSLFYIFNGLLSSISDNVFVGTIYINEAKAAMESGAITLKQYELLAVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTLVLTLVGLLCVEFTLAPVTEWFMQMGWIATL |
cell cycle cell division peptidoglycan metabolic process | plasma membrane | protein homodimerization activity protein-macromolecule adaptor activity | Escherichia coli | 3D-structure Cell cycle Cell division Cell membrane Direct protein sequencing Lipoprotein Membrane Palmitate Reference proteome Repeat Signal TPR repeat | MKPFLRWCFV | MKPFLRWCFVATALTLAGCSNTSWRKSEVLAVPLQPTLQQEVILARMEQILASRALTDDERAQLLYERGVLYDSLGLRALARNDFSQALAIRPDMPEVFNYLGIYLTQAGNFDAAYEAFDSVLELDPTYNYAHLNRGIALYYGGRDKLAQDDLLAFYQDDPNDPFRSLWLYLAEQKLDEKQAKEVLKQHFEKSDKEQWGWNIVEFYLGNISEQTLMERLKADATDNTSLAEHLSETNFYLGKYYLSLGDLDSATALFKLAVANNVHNFVEHRYALLELSLLGQDQDDLAESDQQ | cell cycle cell division peptidoglycan metabolic process plasma membrane protein homodimerization activity protein-macromolecule adaptor activity Escherichia coli 3D-structure Cell cycle Cell division Cell membrane Direct protein sequencing Lipoprotein Membrane Palmitate Reference proteome Repeat Signal TPR repeat MKPFLRWCFV MKPFLRWCFVATALTLAGCSNTSWRKSEVLAVPLQPTLQQEVILARMEQILASRALTDDERAQLLYERGVLYDSLGLRALARNDFSQALAIRPDMPEVFNYLGIYLTQAGNFDAAYEAFDSVLELDPTYNYAHLNRGIALYYGGRDKLAQDDLLAFYQDDPNDPFRSLWLYLAEQKLDEKQAKEVLKQHFEKSDKEQWGWNIVEFYLGNISEQTLMERLKADATDNTSLAEHLSETNFYLGKYYLSLGDLDSATALFKLAVANNVHNFVEHRYALLELSLLGQDQDDLAESDQQ |
nitrogen fixation regulation of DNA-templated transcription regulation of nitrogen compound metabolic process signal transduction involved in regulation of gene expression | cytoplasm | ATP binding identical protein binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity phosphotransferase activity, carboxyl group as acceptor protein histidine kinase activity protein homodimerization activity | Escherichia coli | 3D-structure ATP-binding Cytoplasm Hydrolase Kinase Nitrogen fixation Nucleotide-binding Phosphoprotein Reference proteome Transferase Two-component regulatory system | MATGTQPDAG | MATGTQPDAGQILNSLINSILLIDDNLAIHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLNIELMQESLEAGQGFTDNEVTLVIDGRSHILSVTAQRMPDGMILLEMAPMDNQRRLSQEQLQHAQQVAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPSLLEYTKVIIEQADRLRNLVDRLLGPQLPGTRVTESIHKVAERVVTLVSMELPDNVRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQALGPEGGEIILRTRTAFQLTLHGERYRLAARIDVEDNGPGIPPHLQDTLFYPMVSGREGGTGLGLSIARNLIDQHSGKIEFTSWPGHTEFSVYLPIRK | nitrogen fixation regulation of DNA-templated transcription regulation of nitrogen compound metabolic process signal transduction involved in regulation of gene expression cytoplasm ATP binding identical protein binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity phosphotransferase activity, carboxyl group as acceptor protein histidine kinase activity protein homodimerization activity Escherichia coli 3D-structure ATP-binding Cytoplasm Hydrolase Kinase Nitrogen fixation Nucleotide-binding Phosphoprotein Reference proteome Transferase Two-component regulatory system MATGTQPDAG MATGTQPDAGQILNSLINSILLIDDNLAIHYANPAAQQLLAQSSRKLFGTPLPELLSYFSLNIELMQESLEAGQGFTDNEVTLVIDGRSHILSVTAQRMPDGMILLEMAPMDNQRRLSQEQLQHAQQVAARDLVRGLAHEIKNPLGGLRGAAQLLSKALPDPSLLEYTKVIIEQADRLRNLVDRLLGPQLPGTRVTESIHKVAERVVTLVSMELPDNVRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQALGPEGGEIILRTRTAFQLTLHGERYRLAARIDVEDNGPGIPPHLQDTLFYPMVSGREGGTGLGLSIARNLIDQHSGKIEFTSWPGHTEFSVYLPIRK |
nitrogen fixation regulation of DNA-templated transcription regulation of nitrogen utilization | cytosol | ATP binding ATP hydrolysis activity phosphorelay response regulator activity sequence-specific DNA binding | Escherichia coli | Activator ATP-binding Cytoplasm DNA-binding Nitrogen fixation Nucleotide-binding Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Two-component regulatory system | MQRGIVWVVD | MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVAESTSQMQPDSWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME | nitrogen fixation regulation of DNA-templated transcription regulation of nitrogen utilization cytosol ATP binding ATP hydrolysis activity phosphorelay response regulator activity sequence-specific DNA binding Escherichia coli Activator ATP-binding Cytoplasm DNA-binding Nitrogen fixation Nucleotide-binding Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Two-component regulatory system MQRGIVWVVD MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGAEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNVQLNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQVAARELGVEAKLLHPETEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGELFESTVAESTSQMQPDSWATLLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME |
nucleoside transmembrane transport | plasma membrane | cytidine transmembrane transporter activity nucleoside:proton symporter activity uridine transmembrane transporter activity | Escherichia coli | Cell inner membrane Cell membrane Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport | MDRVLHFVLA | MDRVLHFVLALAVVAILALLVSSDRKKIRIRYVIQLLVIEVLLAWFFLNSDVGLGFVKGFSEMFEKLLGFANEGTNFVFGSMNDQGLAFFFLKVLCPIVFISALIGILQHIRVLPVIIRAIGFLLSKVNGMGKLESFNAVSSLILGQSENFIAYKDILGKISRNRMYTMAATAMSTVSMSIVGAYMTMLEPKYVVAALVLNMFSTFIVLSLINPYRVDASEENIQMSNLHEGQSFFEMLGEYILAGFKVAIIVAAMLIGFIALIAALNALFATVTGWFGYSISFQGILGYIFYPIAWVMGVPSSEALQVGSIMATKLVSNEFVAMMDLQKIASTLSPRAEGIISVFLVSFANFSSIGIIAGAVKGLNEEQGNVVSRFGLKLVYGSTLVSVLSASIAALVL | nucleoside transmembrane transport plasma membrane cytidine transmembrane transporter activity nucleoside:proton symporter activity uridine transmembrane transporter activity Escherichia coli Cell inner membrane Cell membrane Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport MDRVLHFVLA MDRVLHFVLALAVVAILALLVSSDRKKIRIRYVIQLLVIEVLLAWFFLNSDVGLGFVKGFSEMFEKLLGFANEGTNFVFGSMNDQGLAFFFLKVLCPIVFISALIGILQHIRVLPVIIRAIGFLLSKVNGMGKLESFNAVSSLILGQSENFIAYKDILGKISRNRMYTMAATAMSTVSMSIVGAYMTMLEPKYVVAALVLNMFSTFIVLSLINPYRVDASEENIQMSNLHEGQSFFEMLGEYILAGFKVAIIVAAMLIGFIALIAALNALFATVTGWFGYSISFQGILGYIFYPIAWVMGVPSSEALQVGSIMATKLVSNEFVAMMDLQKIASTLSPRAEGIISVFLVSFANFSSIGIIAGAVKGLNEEQGNVVSRFGLKLVYGSTLVSVLSASIAALVL |
adenosine transport nucleoside transmembrane transport organic substance transport purine nucleoside transmembrane transport pyrimidine nucleoside transport uridine transport | plasma membrane | cytidine transmembrane transporter activity nucleoside:proton symporter activity pyrimidine nucleoside transmembrane transporter activity uridine transmembrane transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Direct protein sequencing Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport | MNLKLQLKIL | MNLKLQLKILSFLQFCLWGSWLTTLGSYMFVTLKFDGASIGAVYSSLGIAAVFMPALLGIVADKWLSAKWVYAICHTIGAITLFMAAQVTTPEAMFLVILINSFAYMPTLGLINTISYYRLQNAGMDIVTDFPPIRIWGTIGFIMAMWVVSLSGFELSHMQLYIGAALSAILVLFTLTLPHIPVAKQQANQSWTTLLGLDAFALFKNKRMAIFFIFSMLLGAELQITNMFGNTFLHSFDKDPMFASSFIVQHASIIMSISQISETLFILTIPFFLSRYGIKNVMMISIVAWILRFALFAYGDPTPFGTVLLVLSMIVYGCAFDFFNISGSVFVEKEVSPAIRASAQGMFLMMTNGFGCILGGIVSGKVVEMYTQNGITDWQTVWLIFAGYSVVLAFAFMAMFKYKHVRVPTGTQTVSH | adenosine transport nucleoside transmembrane transport organic substance transport purine nucleoside transmembrane transport pyrimidine nucleoside transport uridine transport plasma membrane cytidine transmembrane transporter activity nucleoside:proton symporter activity pyrimidine nucleoside transmembrane transporter activity uridine transmembrane transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Direct protein sequencing Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport MNLKLQLKIL MNLKLQLKILSFLQFCLWGSWLTTLGSYMFVTLKFDGASIGAVYSSLGIAAVFMPALLGIVADKWLSAKWVYAICHTIGAITLFMAAQVTTPEAMFLVILINSFAYMPTLGLINTISYYRLQNAGMDIVTDFPPIRIWGTIGFIMAMWVVSLSGFELSHMQLYIGAALSAILVLFTLTLPHIPVAKQQANQSWTTLLGLDAFALFKNKRMAIFFIFSMLLGAELQITNMFGNTFLHSFDKDPMFASSFIVQHASIIMSISQISETLFILTIPFFLSRYGIKNVMMISIVAWILRFALFAYGDPTPFGTVLLVLSMIVYGCAFDFFNISGSVFVEKEVSPAIRASAQGMFLMMTNGFGCILGGIVSGKVVEMYTQNGITDWQTVWLIFAGYSVVLAFAFMAMFKYKHVRVPTGTQTVSH |
DNA-templated transcription termination protein complex oligomerization regulation of DNA-templated transcription elongation ribosome biogenesis transcription antitermination | cytosol; transcription elongation factor complex | bacterial-type RNA polymerase core enzyme binding DNA-binding transcription factor activity nucleotide binding protein domain specific binding RNA binding | Escherichia coli | 3D-structure Cytoplasm Direct protein sequencing Host-virus interaction Reference proteome Repeat Ribosome biogenesis RNA-binding Stress response Transcription Transcription antitermination Transcription regulation Transcription termination | MNKEILAVVE | MNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVQIDRKSGDFDTFRRWLVVDEVTQPTKEITLEAARYEDESLNLGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNISLDLGNNAEAVILREDMLPRENFRPGDRVRGVLYSVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVIEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGRNGQNVRLASQLSGWELNVMTVDDLQAKHQAEAHAAIDTFTKYLDIDEDFATVLVEEGFSTLEELAYVPMKELLEIEGLDEPTVEALRERAKNALATIAQAQEESLGDNKPADDLLNLEGVDRDLAFKLAARGVCTLEDLAEQGIDDLADIEGLTDEKAGALIMAARNICWFGDEA | DNA-templated transcription termination protein complex oligomerization regulation of DNA-templated transcription elongation ribosome biogenesis transcription antitermination cytosol; transcription elongation factor complex bacterial-type RNA polymerase core enzyme binding DNA-binding transcription factor activity nucleotide binding protein domain specific binding RNA binding Escherichia coli 3D-structure Cytoplasm Direct protein sequencing Host-virus interaction Reference proteome Repeat Ribosome biogenesis RNA-binding Stress response Transcription Transcription antitermination Transcription regulation Transcription termination MNKEILAVVE MNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVQIDRKSGDFDTFRRWLVVDEVTQPTKEITLEAARYEDESLNLGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNISLDLGNNAEAVILREDMLPRENFRPGDRVRGVLYSVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVIEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGRNGQNVRLASQLSGWELNVMTVDDLQAKHQAEAHAAIDTFTKYLDIDEDFATVLVEEGFSTLEELAYVPMKELLEIEGLDEPTVEALRERAKNALATIAQAQEESLGDNKPADDLLNLEGVDRDLAFKLAARGVCTLEDLAEQGIDDLADIEGLTDEKAGALIMAARNICWFGDEA |
tricarboxylic acid cycle | cytoplasm; cytosol; oxoglutarate dehydrogenase complex | identical protein binding magnesium ion binding nucleotide binding oxoglutarate dehydrogenase (succinyl-transferring) activity thiamine pyrophosphate binding | Escherichia coli | 3D-structure Nucleotide-binding Oxidoreductase Phosphoprotein Reference proteome Thiamine pyrophosphate Tricarboxylic acid cycle | MQNSALKAWL | MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHSQTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKVADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEEKRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDFQTDGGLVHLALAFNPSHLEIVSPVVIGSVRARLDRLDEPSSNKVLPITIHGDAAVTGQGVVQETLNMSKARGYEVGGTVRIVINNQVGFTTSNPLDARSTPYCTDIGKMVQAPIFHVNADDPEAVAFVTRLALDFRNTFKRDVFIDLVCYRRHGHNEADEPSATQPLMYQKIKKHPTPRKIYADKLEQEKVATLEDATEMVNLYRDALDAGDCVVAEWRPMNMHSFTWSPYLNHEWDEEYPNKVEMKRLQELAKRISTVPEAVEMQSRVAKIYGDRQAMAAGEKLFDWGGAENLAYATLVDEGIPVRLSGEDSGRGTFFHRHAVIHNQSNGSTYTPLQHIHNGQGAFRVWDSVLSEEAVLAFEYGYATAEPRTLTIWEAQFGDFANGAQVVIDQFISSGEQKWGRMCGLVMLLPHGYEGQGPEHSSARLERYLQLCAEQNMQVCVPSTPAQVYHMLRRQALRGMRRPLVVMSPKSLLRHPLAVSSLEELANGTFLPAIGEIDELDPKGVKRVVMCSGKVYYDLLEQRRKNNQHDVAIVRIEQLYPFPHKAMQEVLQQFAHVKDFVWCQEEPLNQGAWYCSQHHFREVIPFGASLRYAGRPASASPAVGYMSVHQKQQQDLVNDALNVE | tricarboxylic acid cycle cytoplasm; cytosol; oxoglutarate dehydrogenase complex identical protein binding magnesium ion binding nucleotide binding oxoglutarate dehydrogenase (succinyl-transferring) activity thiamine pyrophosphate binding Escherichia coli 3D-structure Nucleotide-binding Oxidoreductase Phosphoprotein Reference proteome Thiamine pyrophosphate Tricarboxylic acid cycle MQNSALKAWL MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHSQTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKVADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEEKRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDFQTDGGLVHLALAFNPSHLEIVSPVVIGSVRARLDRLDEPSSNKVLPITIHGDAAVTGQGVVQETLNMSKARGYEVGGTVRIVINNQVGFTTSNPLDARSTPYCTDIGKMVQAPIFHVNADDPEAVAFVTRLALDFRNTFKRDVFIDLVCYRRHGHNEADEPSATQPLMYQKIKKHPTPRKIYADKLEQEKVATLEDATEMVNLYRDALDAGDCVVAEWRPMNMHSFTWSPYLNHEWDEEYPNKVEMKRLQELAKRISTVPEAVEMQSRVAKIYGDRQAMAAGEKLFDWGGAENLAYATLVDEGIPVRLSGEDSGRGTFFHRHAVIHNQSNGSTYTPLQHIHNGQGAFRVWDSVLSEEAVLAFEYGYATAEPRTLTIWEAQFGDFANGAQVVIDQFISSGEQKWGRMCGLVMLLPHGYEGQGPEHSSARLERYLQLCAEQNMQVCVPSTPAQVYHMLRRQALRGMRRPLVVMSPKSLLRHPLAVSSLEELANGTFLPAIGEIDELDPKGVKRVVMCSGKVYYDLLEQRRKNNQHDVAIVRIEQLYPFPHKAMQEVLQQFAHVKDFVWCQEEPLNQGAWYCSQHHFREVIPFGASLRYAGRPASASPAVGYMSVHQKQQQDLVNDALNVE |
L-lysine catabolic process to acetyl-CoA via saccharopine tricarboxylic acid cycle | cytoplasm; cytosol; oxoglutarate dehydrogenase complex | dihydrolipoyllysine-residue succinyltransferase activity lipoic acid binding | Escherichia coli | 3D-structure Acetylation Acyltransferase Direct protein sequencing Lipoyl Reference proteome Transferase Tricarboxylic acid cycle | MSSVDILVPD | MSSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLDV | L-lysine catabolic process to acetyl-CoA via saccharopine tricarboxylic acid cycle cytoplasm; cytosol; oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase activity lipoic acid binding Escherichia coli 3D-structure Acetylation Acyltransferase Direct protein sequencing Lipoyl Reference proteome Transferase Tricarboxylic acid cycle MSSVDILVPD MSSVDILVPDLPESVADATVATWHKKPGDAVVRDEVLVEIETDKVVLEVPASADGILDAVLEDEGTTVTSRQILGRLREGNSAGKETSAKSEEKASTPAQRQQASLEEQNNDALSPAIRRLLAEHNLDASAIKGTGVGGRLTREDVEKHLAKAPAKESAPAAAAPAAQPALAARSEKRVPMTRLRKRVAERLLEAKNSTAMLTTFNEVNMKPIMDLRKQYGEAFEKRHGIRLGFMSFYVKAVVEALKRYPEVNASIDGDDVVYHNYFDVSMAVSTPRGLVTPVLRDVDTLGMADIEKKIKELAVKGRDGKLTVEDLTGGNFTITNGGVFGSLMSTPIINPPQSAILGMHAIKDRPMAVNGQVEILPMMYLALSYDHRLIDGRESVGFLVTIKELLEDPTRLLLDV |
glycolytic process pyruvate catabolic process | cytosol; cytosolic pyruvate dehydrogenase complex; membrane; pyruvate dehydrogenase complex | identical protein binding magnesium ion binding molecular adaptor activity protein homodimerization activity pyruvate dehydrogenase (acetyl-transferring) activity pyruvate dehydrogenase activity small molecule binding thiamine pyrophosphate binding | Escherichia coli | 3D-structure Acetylation Direct protein sequencing Glycolysis Magnesium Metal-binding Oxidoreductase Pyruvate Reference proteome Thiamine pyrophosphate | MSERFPNDVD | MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRHIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA | glycolytic process pyruvate catabolic process cytosol; cytosolic pyruvate dehydrogenase complex; membrane; pyruvate dehydrogenase complex identical protein binding magnesium ion binding molecular adaptor activity protein homodimerization activity pyruvate dehydrogenase (acetyl-transferring) activity pyruvate dehydrogenase activity small molecule binding thiamine pyrophosphate binding Escherichia coli 3D-structure Acetylation Direct protein sequencing Glycolysis Magnesium Metal-binding Oxidoreductase Pyruvate Reference proteome Thiamine pyrophosphate MSERFPNDVD MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRHIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA |
chromosome segregation DNA topological change plasmid partitioning sister chromatid cohesion | chromosome; cytoplasm; cytosol; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; extrinsic component of plasma membrane | ATP binding DNA binding DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | Escherichia coli | 3D-structure Cell membrane Direct protein sequencing DNA-binding Isomerase Membrane Reference proteome Topoisomerase | MSDMAERLAL | MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE | chromosome segregation DNA topological change plasmid partitioning sister chromatid cohesion chromosome; cytoplasm; cytosol; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; extrinsic component of plasma membrane ATP binding DNA binding DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity Escherichia coli 3D-structure Cell membrane Direct protein sequencing DNA-binding Isomerase Membrane Reference proteome Topoisomerase MSDMAERLAL MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE |
cell wall organization FtsZ-dependent cytokinesis peptidoglycan biosynthetic process peptidoglycan metabolic process proteolysis regulation of cell shape response to xenobiotic stimulus | periplasmic space | endopeptidase activity serine-type D-Ala-D-Ala carboxypeptidase activity | Escherichia coli | Cell shape Cell wall biogenesis/degradation Direct protein sequencing Hydrolase Peptidoglycan synthesis Periplasm Reference proteome Signal | MPKFRVSLFS | MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQMAAAGQTAQND | cell wall organization FtsZ-dependent cytokinesis peptidoglycan biosynthetic process peptidoglycan metabolic process proteolysis regulation of cell shape response to xenobiotic stimulus periplasmic space endopeptidase activity serine-type D-Ala-D-Ala carboxypeptidase activity Escherichia coli Cell shape Cell wall biogenesis/degradation Direct protein sequencing Hydrolase Peptidoglycan synthesis Periplasm Reference proteome Signal MPKFRVSLFS MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPDLVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTKLLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGHCLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQMAAAGQTAQND |
de novo' pyridoxal 5'-phosphate biosynthetic process pyridoxal phosphate biosynthetic process pyridoxine biosynthetic process | cytosol; protein-containing complex | FMN binding oxidoreductase activity phosphate ion binding protein homodimerization activity pyridoxal phosphate binding pyridoxamine phosphate oxidase activity riboflavin binding | Escherichia coli | 3D-structure Direct protein sequencing Flavoprotein FMN Oxidoreductase Pyridoxine biosynthesis Reference proteome | MSDNDELQQI | MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP | de novo' pyridoxal 5'-phosphate biosynthetic process pyridoxal phosphate biosynthetic process pyridoxine biosynthetic process cytosol; protein-containing complex FMN binding oxidoreductase activity phosphate ion binding protein homodimerization activity pyridoxal phosphate binding pyridoxamine phosphate oxidase activity riboflavin binding Escherichia coli 3D-structure Direct protein sequencing Flavoprotein FMN Oxidoreductase Pyridoxine biosynthesis Reference proteome MSDNDELQQI MSDNDELQQIAHLRREYTKGGLRRRDLPADPLTLFERWLSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLSTLEVMKYFHSRPRDSQIGAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP |
magnesium ion homeostasis phosphate ion transmembrane transport tellurite transport | plasma membrane | inorganic phosphate transmembrane transporter activity solute:proton symporter activity tellurite transmembrane transporter activity zinc ion transmembrane transporter activity | Escherichia coli | Cell inner membrane Cell membrane Ion transport Magnesium Membrane Phosphate transport Reference proteome Symport Transmembrane Transmembrane helix Transport Zinc Zinc transport | MLHLFAGLDL | MLHLFAGLDLHTGLLLLLALAFVLFYEAINGFHDTANAVATVIYTRAMRSQLAVVMAAVFNFLGVLLGGLSVAYAIVHMLPTDLLLNMGSSHGLAMVFSMLLAAIIWNLGTWYFGLPASSSHTLIGAIIGIGLTNALMTGTSVVDALNIPKVLSIFGSLIVSPIVGLVFAGGLIFLLRRYWSGTKKRARIHLTPAEREKKDGKKKPPFWTRIALILSAIGVAFSHGANDGQKGIGLVMLVLIGVAPAGFVVNMNATGYEITRTRDAINNVEAYFEQHPALLKQATGADQLVPAPEAGATQPAEFHCHPSNTINALNRLKGMLTTDVESYDKLSLDQRSQMRRIMLCVSDTIDKVVKMPGVSADDQRLLKKLKSDMLSTIEYAPVWIIMAVALALGIGTMIGWRRVATTIGEKIGKKGMTYAQGMSAQMTAAVSIGLASYTGMPVSTTHVLSSSVAGTMVVDGGGLQRKTVTSILMAWVFTLPAAVLLSGGLYWLSLQFL | magnesium ion homeostasis phosphate ion transmembrane transport tellurite transport plasma membrane inorganic phosphate transmembrane transporter activity solute:proton symporter activity tellurite transmembrane transporter activity zinc ion transmembrane transporter activity Escherichia coli Cell inner membrane Cell membrane Ion transport Magnesium Membrane Phosphate transport Reference proteome Symport Transmembrane Transmembrane helix Transport Zinc Zinc transport MLHLFAGLDL MLHLFAGLDLHTGLLLLLALAFVLFYEAINGFHDTANAVATVIYTRAMRSQLAVVMAAVFNFLGVLLGGLSVAYAIVHMLPTDLLLNMGSSHGLAMVFSMLLAAIIWNLGTWYFGLPASSSHTLIGAIIGIGLTNALMTGTSVVDALNIPKVLSIFGSLIVSPIVGLVFAGGLIFLLRRYWSGTKKRARIHLTPAEREKKDGKKKPPFWTRIALILSAIGVAFSHGANDGQKGIGLVMLVLIGVAPAGFVVNMNATGYEITRTRDAINNVEAYFEQHPALLKQATGADQLVPAPEAGATQPAEFHCHPSNTINALNRLKGMLTTDVESYDKLSLDQRSQMRRIMLCVSDTIDKVVKMPGVSADDQRLLKKLKSDMLSTIEYAPVWIIMAVALALGIGTMIGWRRVATTIGEKIGKKGMTYAQGMSAQMTAAVSIGLASYTGMPVSTTHVLSSSVAGTMVVDGGGLQRKTVTSILMAWVFTLPAAVLLSGGLYWLSLQFL |
protein folding | outer membrane-bounded periplasmic space; periplasmic space | peptidyl-prolyl cis-trans isomerase activity | Escherichia coli | 3D-structure Direct protein sequencing Isomerase Periplasm Reference proteome Rotamase Signal | MFKSTLAAMA | MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP | protein folding outer membrane-bounded periplasmic space; periplasmic space peptidyl-prolyl cis-trans isomerase activity Escherichia coli 3D-structure Direct protein sequencing Isomerase Periplasm Reference proteome Rotamase Signal MFKSTLAAMA MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAKVLP |
polyphosphate catabolic process | plasma membrane | exopolyphosphatase activity guanosine tetraphosphate binding identical protein binding protein homodimerization activity | Escherichia coli | 3D-structure Cell membrane Direct protein sequencing Hydrolase Magnesium Membrane Reference proteome | MPIHDKSPRP | MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTASSLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNALVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA | polyphosphate catabolic process plasma membrane exopolyphosphatase activity guanosine tetraphosphate binding identical protein binding protein homodimerization activity Escherichia coli 3D-structure Cell membrane Direct protein sequencing Hydrolase Magnesium Membrane Reference proteome MPIHDKSPRP MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTASSLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNALVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA |
amino acid import across plasma membrane cellular response to osmotic stress glycine betaine transport glycine import across plasma membrane hyperosmotic response | membrane; outer membrane-bounded periplasmic space; ProVWX complex | quaternary ammonium group binding transmembrane transporter activity | Escherichia coli | 3D-structure Amino-acid transport Direct protein sequencing Disulfide bond Periplasm Reference proteome Signal Transport | MRHSVLFATA | MRHSVLFATAFATLISTQTFAADLPGKGITVNPVQSTITEETFQTLLVSRALEKLGYTVNKPSEVDYNVGYTSLASGDATFTAVNWTPLHDNMYEAAGGDKKFYREGVFVNGAAQGYLIDKKTADQYKITNIAQLKDPKIAKLFDTNGDGKADLTGCNPGWGCEGAINHQLAAYELTNTVTHNQGNYAAMMADTISRYKEGKPVFYYTWTPYWVSNELKPGKDVVWLQVPFSALPGDKNADTKLPNGANYGFPVSTMHIVANKAWAEKNPAAAKLFAIMQLPVADINAQNAIMHDGKASEGDIQGHVDGWIKAHQQQFDGWVNEALAAQK | amino acid import across plasma membrane cellular response to osmotic stress glycine betaine transport glycine import across plasma membrane hyperosmotic response membrane; outer membrane-bounded periplasmic space; ProVWX complex quaternary ammonium group binding transmembrane transporter activity Escherichia coli 3D-structure Amino-acid transport Direct protein sequencing Disulfide bond Periplasm Reference proteome Signal Transport MRHSVLFATA MRHSVLFATAFATLISTQTFAADLPGKGITVNPVQSTITEETFQTLLVSRALEKLGYTVNKPSEVDYNVGYTSLASGDATFTAVNWTPLHDNMYEAAGGDKKFYREGVFVNGAAQGYLIDKKTADQYKITNIAQLKDPKIAKLFDTNGDGKADLTGCNPGWGCEGAINHQLAAYELTNTVTHNQGNYAAMMADTISRYKEGKPVFYYTWTPYWVSNELKPGKDVVWLQVPFSALPGDKNADTKLPNGANYGFPVSTMHIVANKAWAEKNPAAAKLFAIMQLPVADINAQNAIMHDGKASEGDIQGHVDGWIKAHQQQFDGWVNEALAAQK |
phage shock regulation of cellular response to stress regulation of DNA-templated transcription response to heat | cell pole; cytosol; plasma membrane; transcription regulator complex | identical protein binding phospholipid binding | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Coiled coil Cytoplasm Direct protein sequencing Membrane Reference proteome Stress response | MGIFSRFADI | MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQASAREVEWQEKAELALLKEREDLARAALIEKQKLTDLIKSLEHEVTLVDDTLARMKKEIGELENKLSETRARQQALMLRHQAANSSRDVRRQLDSGKLDEAMARFESFERRIDQMEAEAESHSFGKQKSLDDQFAELKADDAISEQLAQLKAKMKQDNQ | phage shock regulation of cellular response to stress regulation of DNA-templated transcription response to heat cell pole; cytosol; plasma membrane; transcription regulator complex identical protein binding phospholipid binding Escherichia coli 3D-structure Cell inner membrane Cell membrane Coiled coil Cytoplasm Direct protein sequencing Membrane Reference proteome Stress response MGIFSRFADI MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQASAREVEWQEKAELALLKEREDLARAALIEKQKLTDLIKSLEHEVTLVDDTLARMKKEIGELENKLSETRARQQALMLRHQAANSSRDVRRQLDSGKLDEAMARFESFERRIDQMEAEAESHSFGKQKSLDDQFAELKADDAISEQLAQLKAKMKQDNQ |
DNA repair protein hexamerization response to ionizing radiation | cell pole; cytoplasm; cytosol | identical protein binding metal ion binding | Escherichia coli | 3D-structure DNA damage DNA repair Metal-binding Reference proteome | MKNTELEQLI | MKNTELEQLINEKLNSAAISDYAPNGLQVEGKETVQKIVTGVTASQALLDEAVRLGADAVIVHHGYFWKGESPVIRGMKRNRLKTLLANDINLYGWHLPLDAHPELGNNAQLAALLGITVMGEIEPLVPWGELTMPVPGLELASWIEARLGRKPLWCGDTGPEVVQRVAWCTGGGQSFIDSAARFGVDAFITGEVSEQTIHSAREQGLHFYAAGHHATERGGIRALSEWLNENTDLDVTFIDIPNPA | DNA repair protein hexamerization response to ionizing radiation cell pole; cytoplasm; cytosol identical protein binding metal ion binding Escherichia coli 3D-structure DNA damage DNA repair Metal-binding Reference proteome MKNTELEQLI MKNTELEQLINEKLNSAAISDYAPNGLQVEGKETVQKIVTGVTASQALLDEAVRLGADAVIVHHGYFWKGESPVIRGMKRNRLKTLLANDINLYGWHLPLDAHPELGNNAQLAALLGITVMGEIEPLVPWGELTMPVPGLELASWIEARLGRKPLWCGDTGPEVVQRVAWCTGGGQSFIDSAARFGVDAFITGEVSEQTIHSAREQGLHFYAAGHHATERGGIRALSEWLNENTDLDVTFIDIPNPA |
nitrogen utilization organonitrogen compound catabolic process pyrimidine nucleobase catabolic process uracil catabolic process | cytosol | deaminase activity identical protein binding | Escherichia coli | Hydrolase Reference proteome | MPKSVIIPAG | MPKSVIIPAGSSAPLAPFVPGTLADGVVYVSGTLAFDQHNNVLFADDPKAQTRHVLETIRKVIETAGGTMADVTFNSIFITDWKNYAAINEIYAEFFPGDKPARFCIQCGLVKPDALVEIATIAHIAK | nitrogen utilization organonitrogen compound catabolic process pyrimidine nucleobase catabolic process uracil catabolic process cytosol deaminase activity identical protein binding Escherichia coli Hydrolase Reference proteome MPKSVIIPAG MPKSVIIPAGSSAPLAPFVPGTLADGVVYVSGTLAFDQHNNVLFADDPKAQTRHVLETIRKVIETAGGTMADVTFNSIFITDWKNYAAINEIYAEFFPGDKPARFCIQCGLVKPDALVEIATIAHIAK |
aspartate transmembrane transport fumarate transport succinate transmembrane transport | plasma membrane | fumarate transmembrane transporter activity L-aspartate transmembrane transporter activity secondary active sulfate transmembrane transporter activity succinate transmembrane transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport | MNKIFSSHVM | MNKIFSSHVMPFRALIDACWKEKYTAARFTRDLIAGITVGIIAIPLAMALAIGSGVAPQYGLYTAAVAGIVIALTGGSRFSVSGPTAAFVVILYPVSQQFGLAGLLVATLLSGIFLILMGLARFGRLIEYIPVSVTLGFTSGIGITIGTMQIKDFLGLQMAHVPEHYLQKVGALFMALPTINVGDAAIGIVTLGILVFWPRLGIRLPGHLPALLAGCAVMGIVNLLGGHVATIGSQFHYVLADGSQGNGIPQLLPQLVLPWDLPNSEFTLTWDSIRTLLPAAFSMAMLGAIESLLCAVVLDGMTGTKHKANSELVGQGLGNIIAPFFGGITATAAIARSAANVRAGATSPISAVIHSILVILALLVLAPLLSWLPLSAMAALLLMVAWNMSEAHKVVDLLRHAPKDDIIVMLLCMSLTVLFDMVIAISVGIVLASLLFMRRIARMTRLAPVVVDVPDDVLVLRVIGPLFFAAAEGLFTDLESRLEGKRIVILKWDAVPVLDAGGLDAFQRFVKRLPEGCELRVCNVEFQPLRTMARAGIQPIPGRLAFFPNRRAAMADL | aspartate transmembrane transport fumarate transport succinate transmembrane transport plasma membrane fumarate transmembrane transporter activity L-aspartate transmembrane transporter activity secondary active sulfate transmembrane transporter activity succinate transmembrane transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport MNKIFSSHVM MNKIFSSHVMPFRALIDACWKEKYTAARFTRDLIAGITVGIIAIPLAMALAIGSGVAPQYGLYTAAVAGIVIALTGGSRFSVSGPTAAFVVILYPVSQQFGLAGLLVATLLSGIFLILMGLARFGRLIEYIPVSVTLGFTSGIGITIGTMQIKDFLGLQMAHVPEHYLQKVGALFMALPTINVGDAAIGIVTLGILVFWPRLGIRLPGHLPALLAGCAVMGIVNLLGGHVATIGSQFHYVLADGSQGNGIPQLLPQLVLPWDLPNSEFTLTWDSIRTLLPAAFSMAMLGAIESLLCAVVLDGMTGTKHKANSELVGQGLGNIIAPFFGGITATAAIARSAANVRAGATSPISAVIHSILVILALLVLAPLLSWLPLSAMAALLLMVAWNMSEAHKVVDLLRHAPKDDIIVMLLCMSLTVLFDMVIAISVGIVLASLLFMRRIARMTRLAPVVVDVPDDVLVLRVIGPLFFAAAEGLFTDLESRLEGKRIVILKWDAVPVLDAGGLDAFQRFVKRLPEGCELRVCNVEFQPLRTMARAGIQPIPGRLAFFPNRRAAMADL |
capsule polysaccharide biosynthetic process cell wall organization peptidoglycan metabolic process peptidoglycan turnover proteolysis septum digestion after cytokinesis | plasma membrane | endopeptidase activity metal ion binding metalloendopeptidase activity | Escherichia coli | Cell inner membrane Cell membrane Cell wall biogenesis/degradation Hydrolase Membrane Metal-binding Metalloprotease Protease Reference proteome Transmembrane Transmembrane helix Zinc | MQQIARSVAL | MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD | capsule polysaccharide biosynthetic process cell wall organization peptidoglycan metabolic process peptidoglycan turnover proteolysis septum digestion after cytokinesis plasma membrane endopeptidase activity metal ion binding metalloendopeptidase activity Escherichia coli Cell inner membrane Cell membrane Cell wall biogenesis/degradation Hydrolase Membrane Metal-binding Metalloprotease Protease Reference proteome Transmembrane Transmembrane helix Zinc MQQIARSVAL MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFAMPQGTPVLSVGDGEVVVAKRSGAAGYYVAIRHGRSYTTRYMHLRKILVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGSDRREFLAQAKEIVPQLRFD |
cysteine transmembrane transport L-cystine transport sulfur utilization | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; plasma membrane | L-cystine transmembrane transporter activity | Escherichia coli | Amino-acid transport Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport | MQESIQLVID | MQESIQLVIDSLPFLLKGAGYTLQLSIGGMFFGLLLGFILALMRLSPIWPVRWLARFYISIFRGTPLIAQLFMIYYGLPQFGIELDPIPSAMIGLSLNTAAYAAETLRAAISSIDKGQWEAAASIGMTPWQTMRRAILPQAARVALPPLSNSFISLVKDTSLAATIQVPELFRQAQLITSRTLEVFTMYLAASLIYWIMATVLSTLQNHFENQLNRQEREPK | cysteine transmembrane transport L-cystine transport sulfur utilization ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; plasma membrane L-cystine transmembrane transporter activity Escherichia coli Amino-acid transport Cell inner membrane Cell membrane Membrane Reference proteome Transmembrane Transmembrane helix Transport MQESIQLVID MQESIQLVIDSLPFLLKGAGYTLQLSIGGMFFGLLLGFILALMRLSPIWPVRWLARFYISIFRGTPLIAQLFMIYYGLPQFGIELDPIPSAMIGLSLNTAAYAAETLRAAISSIDKGQWEAAASIGMTPWQTMRRAILPQAARVALPPLSNSFISLVKDTSLAATIQVPELFRQAQLITSRTLEVFTMYLAASLIYWIMATVLSTLQNHFENQLNRQEREPK |
DNA-templated transcription phosphorelay signal transduction system positive regulation of DNA-templated transcription | cytoplasm | ATP binding ATP hydrolysis activity cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity phosphorelay response regulator activity | Escherichia coli | ATP-binding Cytoplasm DNA-binding Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system | MSHKPAHLLL | MSHKPAHLLLVDDDPGLLKLLGLRLTSEGYSVVTAESGAEGLRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYQAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARLVAQSDVSVLINGQSGTGKEIFAQAIHNASPRNSKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE | DNA-templated transcription phosphorelay signal transduction system positive regulation of DNA-templated transcription cytoplasm ATP binding ATP hydrolysis activity cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity phosphorelay response regulator activity Escherichia coli ATP-binding Cytoplasm DNA-binding Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system MSHKPAHLLL MSHKPAHLLLVDDDPGLLKLLGLRLTSEGYSVVTAESGAEGLRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYQAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARLVAQSDVSVLINGQSGTGKEIFAQAIHNASPRNSKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE |
capsule polysaccharide biosynthetic process cell wall organization peptidoglycan metabolic process peptidoglycan turnover proteolysis | cell outer membrane | cysteine-type peptidase activity endopeptidase activity muramoyltetrapeptide carboxypeptidase activity | Escherichia coli | 3D-structure Cell outer membrane Cell wall biogenesis/degradation Hydrolase Lipoprotein Membrane Palmitate Protease Reference proteome Signal Thiol protease | MVKSQPILRY | MVKSQPILRYILRGIPAIAVAVLLSACSANNTAKNMHPETRAVGSETSSLQASQDEFENLVRNVDVKSRIMDQYADWKGVRYRLGGSTKKGIDCSGFVQRTFREQFGLELPRSTYEQQEMGKSVSRSNLRTGDLVLFRAGSTGRHVGIYIGNNQFVHASTSSGVIISSMNEPYWKKRYNEARRVLSRS | capsule polysaccharide biosynthetic process cell wall organization peptidoglycan metabolic process peptidoglycan turnover proteolysis cell outer membrane cysteine-type peptidase activity endopeptidase activity muramoyltetrapeptide carboxypeptidase activity Escherichia coli 3D-structure Cell outer membrane Cell wall biogenesis/degradation Hydrolase Lipoprotein Membrane Palmitate Protease Reference proteome Signal Thiol protease MVKSQPILRY MVKSQPILRYILRGIPAIAVAVLLSACSANNTAKNMHPETRAVGSETSSLQASQDEFENLVRNVDVKSRIMDQYADWKGVRYRLGGSTKKGIDCSGFVQRTFREQFGLELPRSTYEQQEMGKSVSRSNLRTGDLVLFRAGSTGRHVGIYIGNNQFVHASTSSGVIISSMNEPYWKKRYNEARRVLSRS |
DNA-templated transcription elongation positive regulation of translation transcription antitermination transcription elongation-coupled chromatin remodeling | cytosol | bacterial-type RNA polymerase core enzyme binding DNA binding regulatory RNA binding transcription antitermination factor activity, DNA binding translation activator activity | Escherichia coli | 3D-structure DNA-binding Reference proteome Transcription Transcription antitermination Transcription regulation | MQSWYLLYCK | MQSWYLLYCKRGQLQRAQEHLERQAVNCLAPMITLEKIVRGKRTAVSEPLFPNYLFVEFDPEVIHTTTINATRGVSHFVRFGASPAIVPSAVIHQLSVYKPKDIVDPATPYPGDKVIITEGAFEGFQAIFTEPDGEARSMLLLNLINKEIKHSVKNTEFRKL | DNA-templated transcription elongation positive regulation of translation transcription antitermination transcription elongation-coupled chromatin remodeling cytosol bacterial-type RNA polymerase core enzyme binding DNA binding regulatory RNA binding transcription antitermination factor activity, DNA binding translation activator activity Escherichia coli 3D-structure DNA-binding Reference proteome Transcription Transcription antitermination Transcription regulation MQSWYLLYCK MQSWYLLYCKRGQLQRAQEHLERQAVNCLAPMITLEKIVRGKRTAVSEPLFPNYLFVEFDPEVIHTTTINATRGVSHFVRFGASPAIVPSAVIHQLSVYKPKDIVDPATPYPGDKVIITEGAFEGFQAIFTEPDGEARSMLLLNLINKEIKHSVKNTEFRKL |
dormancy process negative regulation of translation negative regulation of translational elongation primary metabolic process | cytosol; cytosolic small ribosomal subunit | ribosomal small subunit binding ribosome binding | Escherichia coli | 3D-structure Direct protein sequencing Reference proteome Translation regulation | MQLNITGNNV | MQLNITGNNVEITEALREFVTAKFAKLEQYFDRINQVYVVLKVEKVTHTSDATLHVNGGEIHASAEGQDMYAAIDGLIDKLARQLTKHKDKLKQH | dormancy process negative regulation of translation negative regulation of translational elongation primary metabolic process cytosol; cytosolic small ribosomal subunit ribosomal small subunit binding ribosome binding Escherichia coli 3D-structure Direct protein sequencing Reference proteome Translation regulation MQLNITGNNV MQLNITGNNVEITEALREFVTAKFAKLEQYFDRINQVYVVLKVEKVTHTSDATLHVNGGEIHASAEGQDMYAAIDGLIDKLARQLTKHKDKLKQH |
negative regulation of DNA-templated transcription | plasma membrane; sigma factor antagonist complex | molecular adaptor activity sigma factor antagonist activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Coiled coil Direct protein sequencing Membrane Reference proteome Signal-anchor Transcription Transcription regulation Transmembrane Transmembrane helix | MQKEQLSALM | MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ | negative regulation of DNA-templated transcription plasma membrane; sigma factor antagonist complex molecular adaptor activity sigma factor antagonist activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Coiled coil Direct protein sequencing Membrane Reference proteome Signal-anchor Transcription Transcription regulation Transmembrane Transmembrane helix MQKEQLSALM MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ |
negative regulation of DNA-templated transcription protein stabilization regulation of polysaccharide biosynthetic process | outer membrane-bounded periplasmic space; plasma membrane; sigma factor antagonist complex | antisigma factor binding identical protein binding lipid binding | Escherichia coli | 3D-structure Lipid-binding Periplasm Reference proteome Signal Transcription Transcription regulation | MKQLWFAMSL | MKQLWFAMSLVTGSLLFSANASATPASGALLQQMNLASQSLNYELSFISINKQGVESLRYRHARLDNRPLAQLLQMDGPRREVVQRGNEISYFEPGLEPFTLNGDYIVDSLPSLIYTDFKRLSPYYDFISVGRTRIADRLCEVIRVVARDGTRYSYIVWMDTESKLPMRVDLLDRDGETLEQFRVIAFNVNQDISSSMQTLAKANLPPLLSVPVGEKAKFSWTPTWLPQGFSEVSSSRRPLPTMDNMPIESRLYSDGLFSFSVNVNRATPSSTDQMLRTGRRTVSTSVRDNAEITIVGELPPQTAKRIAENIKFGAAQ | negative regulation of DNA-templated transcription protein stabilization regulation of polysaccharide biosynthetic process outer membrane-bounded periplasmic space; plasma membrane; sigma factor antagonist complex antisigma factor binding identical protein binding lipid binding Escherichia coli 3D-structure Lipid-binding Periplasm Reference proteome Signal Transcription Transcription regulation MKQLWFAMSL MKQLWFAMSLVTGSLLFSANASATPASGALLQQMNLASQSLNYELSFISINKQGVESLRYRHARLDNRPLAQLLQMDGPRREVVQRGNEISYFEPGLEPFTLNGDYIVDSLPSLIYTDFKRLSPYYDFISVGRTRIADRLCEVIRVVARDGTRYSYIVWMDTESKLPMRVDLLDRDGETLEQFRVIAFNVNQDISSSMQTLAKANLPPLLSVPVGEKAKFSWTPTWLPQGFSEVSSSRRPLPTMDNMPIESRLYSDGLFSFSVNVNRATPSSTDQMLRTGRRTVSTSVRDNAEITIVGELPPQTAKRIAENIKFGAAQ |
microcin B17 transport microcin transport peptide transport protein transport response to antibiotic toxin transport | plasma membrane | ATP binding microcin transmembrane transporter activity peptide transmembrane transporter activity protein homodimerization activity secondary active transmembrane transporter activity toxin transmembrane transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Peptide transport Protein transport Reference proteome Transmembrane Transmembrane helix Transport | MFKSFFPKPG | MFKSFFPKPGTFFLSAFVWALIAVIFWQAGGGDWVARITGASGQIPISAARFWSLDFLIFYAYYIVCVGLFALFWFIYSPHRWQYWSILGTALIIFVTWFLVEVGVAVNAWYAPFYDLIQTALSSPHKVTIEQFYREVGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMANWQQLRHIEGAAQRVQEDTMRFASTLENMGVSFINAIMTLIAFLPVLVTLSAHVPELPIIGHIPYGLVIAAIVWSLMGTGLLAVVGIKLPGLEFKNQRVEAAYRKELVYGEDDATRATPPTVRELFSAVRKNYFRLYFHYMYFNIARILYLQVDNVFGLFLLFPSIVAGTITLGLMTQITNVFGQVRGAFQYLINSWTTLVELMSIYKRLRSFEHELDGDKIQEVTHTLS | microcin B17 transport microcin transport peptide transport protein transport response to antibiotic toxin transport plasma membrane ATP binding microcin transmembrane transporter activity peptide transmembrane transporter activity protein homodimerization activity secondary active transmembrane transporter activity toxin transmembrane transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Peptide transport Protein transport Reference proteome Transmembrane Transmembrane helix Transport MFKSFFPKPG MFKSFFPKPGTFFLSAFVWALIAVIFWQAGGGDWVARITGASGQIPISAARFWSLDFLIFYAYYIVCVGLFALFWFIYSPHRWQYWSILGTALIIFVTWFLVEVGVAVNAWYAPFYDLIQTALSSPHKVTIEQFYREVGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMANWQQLRHIEGAAQRVQEDTMRFASTLENMGVSFINAIMTLIAFLPVLVTLSAHVPELPIIGHIPYGLVIAAIVWSLMGTGLLAVVGIKLPGLEFKNQRVEAAYRKELVYGEDDATRATPPTVRELFSAVRKNYFRLYFHYMYFNIARILYLQVDNVFGLFLLFPSIVAGTITLGLMTQITNVFGQVRGAFQYLINSWTTLVELMSIYKRLRSFEHELDGDKIQEVTHTLS |
negative regulation of DNA-templated DNA replication initiation nucleoid organization regulation of DNA-templated transcription response to radiation sister chromatid cohesion | cytosol; protein-containing complex; SeqA-DNA complex | DNA replication origin binding double-stranded methylated DNA binding hemi-methylated DNA-binding identical protein binding protein homodimerization activity | Escherichia coli | 3D-structure Cytoplasm DNA replication inhibitor DNA-binding Reference proteome | MKTIEVDDEL | MKTIEVDDELYSYIASHTKHIGESASDILRRMLKFSAASQPAAPVTKEVRVASPAIVEAKPVKTIKDKVRAMRELLLSDEYAEQKRAVNRFMLLLSTLYSLDAQAFAEATESLHGRTRVYFAADEQTLLKNGNQTKPKHVPGTPYWVITNTNTGRKCSMIEHIMQSMQFPAELIEKVCGTI | negative regulation of DNA-templated DNA replication initiation nucleoid organization regulation of DNA-templated transcription response to radiation sister chromatid cohesion cytosol; protein-containing complex; SeqA-DNA complex DNA replication origin binding double-stranded methylated DNA binding hemi-methylated DNA-binding identical protein binding protein homodimerization activity Escherichia coli 3D-structure Cytoplasm DNA replication inhibitor DNA-binding Reference proteome MKTIEVDDEL MKTIEVDDELYSYIASHTKHIGESASDILRRMLKFSAASQPAAPVTKEVRVASPAIVEAKPVKTIKDKVRAMRELLLSDEYAEQKRAVNRFMLLLSTLYSLDAQAFAEATESLHGRTRVYFAADEQTLLKNGNQTKPKHVPGTPYWVITNTNTGRKCSMIEHIMQSMQFPAELIEKVCGTI |
positive regulation of ATP-dependent activity positive regulation of protein catabolic process positive regulation of proteolysis involved in protein catabolic process | cytosol; HslUV protease complex; ribosome | ATPase binding molecular adaptor activity protein homodimerization activity RNA binding | Escherichia coli | 3D-structure Direct protein sequencing Reference proteome Stress response | MDLSQLTPRR | MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK | positive regulation of ATP-dependent activity positive regulation of protein catabolic process positive regulation of proteolysis involved in protein catabolic process cytosol; HslUV protease complex; ribosome ATPase binding molecular adaptor activity protein homodimerization activity RNA binding Escherichia coli 3D-structure Direct protein sequencing Reference proteome Stress response MDLSQLTPRR MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK |
pentose catabolic process pentose-phosphate shunt, non-oxidative branch | cytosol | D-ribulose-phosphate 3-epimerase activity ferrous iron binding metal ion binding | Escherichia coli | Carbohydrate metabolism Cobalt Iron Isomerase Manganese Metal-binding Reference proteome Zinc | MKQYLIAPSI | MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITAPIDVHLMVKPVDRIVPDFAAAGASIITFHPEASEHVDRTLQLIKENGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRIDESGFDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRSELAKVSHE | pentose catabolic process pentose-phosphate shunt, non-oxidative branch cytosol D-ribulose-phosphate 3-epimerase activity ferrous iron binding metal ion binding Escherichia coli Carbohydrate metabolism Cobalt Iron Isomerase Manganese Metal-binding Reference proteome Zinc MKQYLIAPSI MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITAPIDVHLMVKPVDRIVPDFAAAGASIITFHPEASEHVDRTLQLIKENGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRIDESGFDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRSELAKVSHE |
DNA damage response DNA repair proteolysis regulation of DNA-templated transcription SOS response translesion synthesis | DNA polymerase V complex | ATP-dependent activity, acting on DNA DNA-directed DNA polymerase activity identical protein binding nucleic acid binding serine-type peptidase activity single-stranded DNA binding | Escherichia coli | 3D-structure Autocatalytic cleavage DNA damage DNA repair Hydrolase Protease Reference proteome Serine protease SOS mutagenesis SOS response | MLFIKPADLR | MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR | DNA damage response DNA repair proteolysis regulation of DNA-templated transcription SOS response translesion synthesis DNA polymerase V complex ATP-dependent activity, acting on DNA DNA-directed DNA polymerase activity identical protein binding nucleic acid binding serine-type peptidase activity single-stranded DNA binding Escherichia coli 3D-structure Autocatalytic cleavage DNA damage DNA repair Hydrolase Protease Reference proteome Serine protease SOS mutagenesis SOS response MLFIKPADLR MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR |
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