entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
Q9R6P9 | THIO_MYCGA | Thioredoxin (Trx) | MKHITNKAELDQLLSTNKKVVVDFYANWCGPCKILGPIFEEVAQDKKDWTFVKVDVDQANEISSEYEIRSIPTVIFFQDGKMADKRIGFIPKNELKELLK | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. |
Q9R6T0 | CCS1_SYNP6 | Cytochrome c biogenesis protein CcsB | MTSDPLASPSFADRWRRGQQLFWTWLADLRLAILLLLAIAIASATGTVIEQGQSLAFYQENYPTDPALFGFLSWRWILSLGLDHVYRAGWFLGLLILFGASLTACTFRRQWPALRAAQRWQFYQEPRQFTKLALSASLPQGKLDSLEPLLLQRRYRLFRADDVLYARRGLAGRVGPILVHAGMLVVLGGAIWGSLGGFYAQEMIPSGETFQVRNIVDAGPWSGSRIPQDWAVKVNRFWIDYAPDGRIDQFYSDLSVVDREGQEQDRQTIHVNQPLRYGGLTFYQADWAIAAAQVRLNNSPVLQLPMAQLPAAGRIWGTFV... | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. {ECO:0000255|HAMAP-Rule:MF_01392}. |
Q9R6T3 | DPSA_SYNP6 | Nutrient stress-induced DNA-binding protein | MTNTGLVQSFSQIEPNVLGLETSVTSQICEGLNRALASFQVLYLQYQKHHFTVQGAEFYSLHEFFEDSYGSVKDHVHDLGERLNGLGGVPVAHPLKLAELTCFAIEEDGVFNCRTMLEHDLAAEQAILSLLRRLTAQVESLGDRATRYLLEGILLKTEERAYHIAHFLAPDSLKLA | Involved in protection of chromosomal DNA from damage under nutrient-limited and oxidative stress conditions. Binds heme (By similarity). |
Q9R6W6 | PSBO_CROS5 | Photosystem II manganese-stabilizing polypeptide (MSP) | MRFRTLLIAFLALCLGLITACSEGPANAVNPQDLTYDEILNTGLANKCPQISEFTRGSIPIEPGQTYFVDDLCLEPQEYFVKEEPVNKRQEAEYVPGKLLTRYTTSLEQISGKITVDEDGVVTFYEEGGIDFQPVTVQLPGGEQVPFFFTIKNLVGKTEPGFSSINSSIDFEGDFRVPSYRGATFLDPKGRGLATGYDNAVALPATADKEDYANVKQTPIGKGSISLQVTKVDQATGEIAGVFDSEQPSDTDLGAKEPVEVKIRGIFYARVTPEA | MSP binds to a putative Mn-binding protein and keeps 2 of the 4 Mn-atoms associated with PSII. |
Q9R6W9 | KDPC_ANASL | Potassium-transporting ATPase KdpC subunit (ATP phosphohydrolase [potassium-transporting] C chain) (Potassium-binding and translocating subunit C) (Potassium-translocating ATPase C chain) | MSLIRELLRAIRITLIFWLITAIIYPLAILVVGQGLFPYQANGSIMQNIEAQPIGSALIGQVFASEQYFHSRPSASRYSQGRRARPTGISGGSNLAPSNPALLNRIIEEANQLREENIQPIEDLIYSSGSGLDPHISIQAASQQIERVARARNVQPDEILRLMNKYTDGRFLWIFGEPGVNVLRLNYALDLQDFNNQQNR | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation... |
Q9R6X2 | KDPA_ANASL | Potassium-transporting ATPase potassium-binding subunit (ATP phosphohydrolase [potassium-transporting] A chain) (Potassium-binding and translocating subunit A) (Potassium-translocating ATPase A chain) | MGLGLLQIGLTLCIVIAITPVLGRYIARVFLEERTILDPLMNPIERSIYVISGVRPKDDMTGWQYIRAILYTNLFMGILVYSLIHYQRLLPWNPNGFGVPRWDIILHTVVSFVTNTDQQHYAGETTLSYFSQVAALGFLMFTSAATGLAVGIAFIRGLTGKKLGNFYIDLTRGITRILLPISVIGAIALVLLGVPQTLGGSLTITTLEGGTQYIARGPVASFEMIKMLGENGGGFFAANSAHPFENPNGATNFIETIAMIAIPAAMIYTYGVFAKNIKQAWLLFWMVFIVFVILVWVAATGELQGNPLVNGTLGIEKPNL... | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunne... |
Q9R6Y2 | CCS1_NOSS1 | Cytochrome c biogenesis protein CcsB | MTTDNSAPTASPWWSLPGKFLRREFLPVLTDLRLAIALLLIIALFSISGTVIEQGQSPAFYQSNYPEHPALFGFLTWKVIQVVGLDHVYRTWWFLSLLVLFGTSLTACTFTRQLPALKTAQRWKYYEEPRQFQKLALSAELDAGSVNSLSQILQNRRYKIFQEKDDILYARKGIVGRIGPIIVHIGIVTILLGSIWGAMTGFIAQEMVPSGETFQVKNIIDAGPLAAGQFPQDWSVRVNRFWIDYTPKGGIDQFYSDMSVLDNQGQEVDHKKIFVNQPLRYHGVTFYQTDWGISGVRVRLNKSPIFQLPMALLNTNGQGR... | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. {ECO:0000255|HAMAP-Rule:MF_01392}. |
Q9R6Z3 | ACP_PHOPR | Acyl carrier protein (ACP) | MSNIEDRVRKIIIEQLGVDEAEVKNEASFVDDLGADSLDTVELVMALEEEFDTEIPDEAAEKITTVQAAIDYVNSASE | Carrier of the growing fatty acid chain in fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. |
Q9R9D5 | RFAQ_ECOLX | Lipopolysaccharide core heptosyltransferase RfaQ (EC 2.-.-.-) | MRFHGDMLLTTPVISSLKKNYPDAKIDVLLYQDTIPILSENPEINALYGIKNKKAKASEKIANFFHLIKVLRANKYDLIVNLTDQWMVAILVRLLNARVKISQDYHHRQSAFWRKSFTHLVPLQGGNVVESNLSVLTPLGVDSLVKQTTMSYPPASWKRMRRELDHAGVGQNYVVIQPTARQIFKCWDNAKFSAVIDALHARGYEVVLTSGPDKDDLACVNEIAQGCQTPPVTALAGKVTFPELGALIDHAQLFIGVDSAPAHIAAAVNTPLISLFGATDHIFWRPWSNNMIQFWAGDYREMPTRDQRDRNEMYLSVIPA... | Catalyzes heptose transfer to the lipopolysaccharide core. It transfers a heptose, called heptose(III), to the heptose(II) of the inner core. |
Q9R9J2 | FENF_BACIU | Malonyl CoA-acyl carrier protein transacylase (MCT) (EC 2.3.1.39) | MNNLAFLFPGQGSQFVGMGKSFWNDFVLAKRLFEEASDAISMDVKKLCFDGDMTELTRTMNAQPAILTVSVIAYQVYMQEIGIKPHFLAGHSLGEYSALVCAGVLSFQEAVKLIRQRGILMQNADPEQLGTMAAITQVYIQPLQDLCTEISTEDFPVGVACMNSDQQHVISGHRQAVEFVIKKAERMGANHTYLNVSAPFHSSMMRSASEQFQTALNQYSFRDAEWPIISNVTAIPYNNGHSVREHLQTHMTMPVRWAESMHYLLLHGVTEVIEMGPKNVLVGLLKKITNHIAAYPLGQTSDLHLLSDSAERNENIVNLR... | Is involved in the mycosubtilin synthetase assembly, by catalyzing the transfer of malonyl groups to a specific acyl-carrier-protein domain on MycA. |
Q9R9M8 | AAU3_RHIME | Protein aau3 | MRLTKQTNYAVRMLMYCAANGEKLSRIPEIARAYGVSELFLFKILQPLTRAGLVETVRGRNGGVRLPRPASEITLFDVVKVTEDSFAMAECFEAGEIDCPLVDSCGLNAALRKALNAFFEVLQGYTIDDLVKARPQINFLLGLEEPVRPQTSAA | Required for growth utilizing PHB cycle intermediates. |
Q9R9N2 | LPSB_RHIME | Lipopolysaccharide core biosynthesis mannosyltransferase LpsB (EC 2.4.-.-) | MVDIRDVEVIAPNFKQRLSGVTSTIIQLVPVQRALGQKIAVLGPGLPKSLPSVRFRDLIHLWKRPEGRPCRVWHARRNVEMLPAILLRDLLRMKLRIVFTSASQRRHTGWSKFLIRRMDAVIATSGRTAAYLDVPNTVILHGIDTKRFQPPFDKTEAKKALGLDPAKKFVGCFGRVRHQKGTDLFVDSMIALLPCRPDWGAIVAGRATGPHLAFESELKERVAKAGLADRILFVGEHTNIPDWYRALDLFVAPQRWEGFGLTPLEAMATGVPVVATDVGAFSELVTGGSEETGLIIAADDLKAMVDAAAAFMDDRPRLAA... | Acts at transfer of mannose group to a 3-deoxy-D-mono octulonic acid (KDO) via an alpha-1,5 linkage. |
Q9R9T9 | SRPR_PSEPU | HTH-type transcriptional regulator SrpR (Solvent efflux pump srpABC operon corepressor) | MARKTAAEAEETRQRIIDAALEVFVAQGVSDATLDQIARKAGVTRGAVYWHFNGKLEVLQAVLASRQHPLELDFTPDLGIERSWEAVVVAMLDAVHSPQSKQFSEILIYQGLDESGLIHNRMVQASDRFLQYIHQVLRHAVTQGELPINLDLQTSIGVFKGLITGLLYEGLRSKDQQAQIIKVALGSFWALLREPPRFLLCEEAQIKQVKSFE | In conjunction with SrpS represses the srpABC operon. |
Q9R9U0 | SRPS_PSEPU | HTH-type transcriptional regulator SrpS (Solvent efflux pump srpABC operon corepressor) | MNQSDENVGKAGGIQVIARAASIMRALGSHPHGLSLAAIAQLVGLPRSTVQRIINALEEEFLVEALGPAGGFRLGPALGQLINQAQSDILSLVKPYLRSLAEELEESVCLASLAGDKIYVLDRIVSERELRVVFPIGINVPAAATAAGKVLLAALPDETLQAALGEQLPVFTSNTLRRKALVKQLSEVRQSGFASDLDEHIDGVCSFATLLDTYLGYYSLAVVMPSSRASKQSDLIKKALLQSKQNIERAIGRASKKAP | In conjunction with SrpR represses the srpABC operon. |
Q9R9U2 | RECA_PSEOL | Protein RecA (Recombinase A) | MDQAKSKALEAALSQIEKQFGKGSIMRLGSDRTMDIDVISTGSLGLDIALGVGGLPRGRIVEIYGPESSGKTTLTLSVIAEAQRQGLTCAFVDAEHALDPIYAAKLGVNIDELLCSQPDTGEQALEIVDILTRSGAVNLIVVDSVAALVPKAEIEGEIGDSHVGLAARMMSQAMRKITGNLKNSNTMCIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRTGAVKEGEEVVGSETRVKVVKNKVAAPFRQAEFQIVYGQGISKAGEIVDLAVANNFVEKSGAWYSFEGNKIGQGKANTMKWLLENKPTMDKLEG... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. {ECO:0000255|HAMAP-Ru... |
Q9R9U8 | ALKN_PSEOL | Putative methyl-accepting chemotaxis AlkN | MNCSLRCRFFLILVMAGFSFFVALFGMRLMHKMAEFAYFEREHVVALSKVYYELHKKEINISFIVGQVQRARRQTTAVNSLWKGDKALLRLLGKGLILELSEASEIKLGLLERYASSIYKDGLNPGHIEEMKRLVSWPYTNSNRFGIEIADISKRVKAYVYFLVVSINCLFFVVIFLLMKKTRSSIDEIVHVMNDMSRGDLTYRTIPSNDEVGKMQSSIIAMGAGVSALIESIKHIQGDLFNSAGEALNISQSTSNDICDQAGKIDEFVSALSQISFAITETSNAANKSSALSSEGRQLAVHGQKAIETAVSSINALSQR... | Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. |
Q9R9Y4 | FTSX_PSEPU | Cell division protein FtsX | MSTTRTPKVSERVAPKPADPQPAKKKRGEDDDGPDFRTLLHAWLESHRASMADSLRRLGKQPIGSFFTCLVMAVALSMPMGLSLLLKNIEQLGGSWQRAAQISLFLKLDAGSRDGEALRDEIKGMPGVADAQYVSREQALEEFQQQSGLGEALRELPDNPLPGVVVVTPTEVDKPALEALRQRLSELPRVEVAQLDLVWVERLAAILKLGDRFVFGLAVMLISALLLVIGNTIRLHIENRRIEIEVIKLVGGTDAYVRRPFLYMGALYGLGAGLLAWGILAFGLNWLNEAVVGLSGLYGSDFALGGVPASDGLSLLIGAV... | Part of the ABC transporter FtsEX involved in cellular division. |
Q9RA11 | SELO_MORMI | Protein adenylyltransferase SelO (EC 2.7.7.108) | MRQKTATITRRDKSFTGHYVPVKPTPIKDPEYVAHSKNLFSELGFADSMAESADFVRMFSGDMSGVPVPMRQVGWASGYALSIYGTEYTQQCPFQTGNGYGDGRAISVLETLIKGQRWEMQLKGGGRTPYCRGADGRAVLRSSIREFLAQDHMHALGVPTSRSLSLYVSKTETVKRPWYSQGSRSENPDMLISEAVAISTRVAPSFIRVGQLELFARRSRSNEHPKAMEELEKIVLHLIDREYADVIDTQLATPEKIVLLAREFRGRLTSMVANWIRVGFCQGNFNSDNCAAGGFTLDYGPFGFCDVFNPYYQPWTGGGN... | Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation). {ECO:0000255|HAMAP-Rule:MF_00692}. |
Q9RA13 | AC4CH_MORMI | N(4)-acetylcytidine amidohydrolase (ac4C amidohydrolase) (EC 3.5.1.135) | MYSCITFFQRLERSILSGNKTATIRDKSDSHYLVGQMLDACTHEDNRKMCQIEILSIEYVTFSELNRAHANAEGLPFLFMLKWIVRKIYPTSNDLFFISFRVVTIDIL | Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C). {ECO:0000255|HAMAP-Rule:MF_00684}. |
Q9RA54 | MUTL_THET8 | DNA mismatch repair protein MutL | MIRPLPPELRGLLARGEVLLTVKDAVRELLENALDAGARRVRVELWGGGLKRLVVEDDGEGIPLEDLPLAVEPYATSKLQDLEGIRTLGFRGQALYALRQAARLRIRSRPRGQLGGGLLLAEGERVEVRPVPAPPGTRVEVEGLFLGEGRDPKGEVRGVLELLKRYLLHHPRLALALFAEGEARLLFPGAGLEEAARLAFGRLLAKRLLPLAYGAGGLEVQGLVSRPEVSRTRPDRLFLAVNGRPVAFPEGLLRRVRRAYRELLPEGHYPVGVLNLFLPQEAFRLRLDARKEEVVLSEEVEALVEEALLALFRRENLARA... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... |
Q9RA57 | RL23_THETH | Large ribosomal subunit protein uL23 (50S ribosomal protein L23) (L*23) | MKTAYDVILAPVLSEKAYAGFAEGKYTFWVHPKATKTEIKNAVETAFKVKVVKVNTLHVRGKKKRLGRYLGKRPDRKKAIVQVAPGQKIEALEGLI | One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}. |
Q9RAA9 | DPO1_RICFE | DNA polymerase I (POL I) (EC 2.7.7.7) | MTQKNTLLLIDGYGFVFRAYYAQQPLTSPKGEPVGALYGFASMLLKLLSDFKPKHVAVVFDSGGKNFRHHIYPEYKANRPPPPEDLVVQLPLVRDVASNLNFPILEKNGYEADDIIATFAAKTAALGEDVVVISSDKDLLQLMGENIKIYDPLKGKYITEDDVVKKFGTTSDKLREVMALIGDRSDNIPGVPSIGPKTASSLITQFGSVENIFNSLEQVSSLKQRETLQNSKEAALISWQLIGLDSNVDLDFQLNNLEWSPPNSDKLTGFLQEYGFKSLYKRAENLFDIKINDHKEIVENKVTEAKEISNASELADFAKK... | In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. |
Q9RAE6 | DADA_RHIL3 | D-amino acid dehydrogenase (EC 1.4.99.-) | MKVIVLGAGIVGVTSAYQLAKAGHDVTVVDRQPGPALETSFANAGEVSFGYCSPWAAPGIPMKAMKWLFMKHAPLILRPKLDMAMLSWMARMLSNCTSERYAINKSRMLRLADYSRIALADLRAETGIAYDERMQGTLQLFRTQQQLEASAKDVKALAADGIPYEVLDRDGCIRFEPALKHVRDKIVGGLLTPKDETGDCFKFTNALAAKAEALGVRFAYGTTIKALDVEAGRVRGVITDRERMSAEAVVVALGSYSPLLLKPLGIRLPVYPVKGYSLTIPIADASRAPESTVMDETYKIAITRLGDRIRVGGMAEISGY... | Oxidative deamination of D-amino acids. {ECO:0000255|HAMAP-Rule:MF_01202}. |
Q9RAJ1 | DHAR_MYCSX | HTH-type transcriptional repressor DhaR | MARTPVRQHLVEKGTQVFLERGYSGSAVQDITAAAEVPKGSFYNHFESKEAFGGQVLQEFFSDLQRTISSTLEDASVPPVRRLQNYFAAIIETLDGQGCLIGNFSVELSPLSDVVRTELLRIFEQWVKPFQKCIIEGQETGSIRRDLAPDLLADFLIASWQGAILRMKIERNREPLDQFLTVVFEALLPSTENISNES | Transcriptional repressor for the dhaA haloalkane dehalogenase gene. |
Q9RAN9 | NODA_MESS7 | Nodulation protein A (EC 2.3.1.-) | MRSAVQWRLCWENDLQLTDHVELSDFFRKIYGRIGSFDAKPFEGGRSWAGARPEVRLIASDAQGIAAHVGILRRFIKVGEVDFLVAELGLYGVRPDLEKLGISFSMRMVHPVLQQLAVPFAFGTVRHAMRSHVERFCREGIAAIVPGVKVRSSRANVHHDLPSTRLEDVIVLVSPIGRSIDEWPPGDVIDRNGSEL | N-acyltransferase required for nodulation. Acts in the production of a small, heat-stable compound (Nod) that stimulates mitosis in various plant protoplasts. {ECO:0000255|HAMAP-Rule:MF_00084}. |
Q9RAU1 | ATPG_LACLM | ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit) | MGASLNEIKTKIASTKKTSQITGAMQMVSAAKLQKAESHAKAFQTYAEKVRKITTDLVSSDNEPAKNPMMIKREVKKTGYLVITSDRGLVGSYNSNILKSVISNIRKRHTNESEYTILALGGTGADFFKARNVKVSYVLRGLSDQPTFEEVRAIVTEAVEEYQAEEFDELYVCYNHHVNSLVSEARMEKMLPISFDEKGDEKASLVTFELEPDRETILNQLLPQYAESMIYGSIVDAKTAEHAAGMTAMRTATDNAHSVINDLTIQYNRARQASITQEITEIVAGASAL | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. {ECO:0000255|HAMAP-Rule:MF_00815}. |
Q9RB10 | DSBA_PECCC | Thiol:disulfide interchange protein DsbA | MKKLWFALIGVVLAFSASAAEFSDGKQYVELDKPATQEPQVLEFFSFYCPHCYQFEQVYHVPDAVKKALPEGTKMTRYHVDFLGPLGKNLTQAWAVAMALGVEDKITPLMFDAVQKTQTVQKPEDIREVFVKAGVSAEEFDGALNSFVVKSLVAQQEKAAADLQLRGVPAMFVNGKYMIKNDGLDTSSMDGYVKQYADVVKFLITKK | Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis. |
Q9RB36 | TRUB_FLAJ1 | tRNA pseudouridine synthase B (EC 5.4.99.25) (tRNA pseudouridine(55) synthase) (Psi55 synthase) (tRNA pseudouridylate synthase) (tRNA-uridine isomerase) | MTPEEYLEGQVLLIDKPLKWSSFQAVNKLKYLLINKVGLPKKFKIGHAGTLDPLATGLLLICTGKFTKKISELQGQAKEYTGTFYIGATTPSYDLETEIDQTFPTEHINEVLIHETVKQFLGEIDQKPPIFSAIKKDGVRLYEHARAGESIEIESRKTTIHEFEITRIALPEIDFRVVCSKGTYIRSLAYDFGKAMNSGSHLTVLRRTKIGDYDVKNAIDITLFEESLQ | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}. |
Q9RBS1 | POPB_RALN1 | Protein PopB | MSHSKIKAGGHGSSGIGNDFTPAKTPAPATPAPQSQQVNDLLGRGVGNALNKSNLGSDSQTWTPGSTMVSLKSRSSSSHKPDTGGDTKPDSTSGGKRKRDDETDPNAETEGGKKKKKRDDENDSSQAGGAGSSAGSSGSPEDALMNIALQRAIQRQTQTRQKMQEAMKIKDDDD | Probably involved in host-pathogen interactions. |
Q9RBS2 | POPC_RALN1 | Protein PopC | MPRDTPQTVPGHSPFWPLFFFTHNNKREARHDLARLSLTLMPILPRLFHRTSRTSSADTQRDARTPPNASPLHGEPGRTPRSRGELGRNLRLRSNAQTSGTPGTPARPQIRASASRTAPSTPQHPQGTEGTRTVPNSPLHNDARVFRERADHTGLSAWRTEMLTRFIEHSRKHGLANDFEQVRVYDRLSRAVDHLKSVLRMSGDSVQLKSLPVPELPDVTFEIAHLKNLETVDCDLHALPATLENLFLLETLSLKGAKNFKALPDAVWRLPALQELKLSETGLKSLPPVGGGSALQRLTIEDSPLEQLPAGFADLDQLAS... | Probably involved in host-pathogen interactions. May interact with plant target proteins may modulate a plant signal transduction pathway. |
Q9RC41 | NSRR_HALH5 | HTH-type transcriptional regulator NsrR | MQLTSYTDYSLRLLLYLALQPKDKLSSVKQVATIYNISYNHLTKVTYELGKLGLIETIKGRNGGIRLAKAPEEINIGAVVKQTEDNLELVECFNHETNTCILNPVCRLKGVLHEALTAYLRVLEQYTLKDLLTNEDELQALLKLKP | Nitric oxide-responsive transcriptional regulator. |
Q9RC52 | CITT_HALH5 | Transcriptional regulatory protein CitT | MTKLYKVLIIEDDFRVAQIQEQMVNDHPYFHVISTCRTGGEALDYLSEKAAALDLILLDVYIPDVKGLELLWAIREKFRDVDIMMVTAAKEVDTVQEALRGGIIDYLLKPVQKEVLHQRLDAYVQKRELFGERRQVSQEELDQLRQVQVRVQVGETPLPKGIDRLTLEKVVNALEEAETQGLTAMEGARLIGASRSTVRRYFEYLIHTKKAKAEVNYGDVGRPERRYFLC | Member of the two-component regulatory system CitT/CitS. |
Q9RC88 | PDXA2_HALH5 | Putative D-threonate 4-phosphate dehydrogenase (EC 1.1.1.408) | MNKKPIIAIPMGDPAGIGPEITVGALNKKELYDVANPVVIGHGDMLEKMLPVMKADLTINRITTVDEAMFEYGTIDVIHLDNLNVAEVKMGTVQAQCGKAAFEYIRHAVQLANDKKVDALATTPINKESLKAAEVPYIGHTEMLADLTKTEDPLTMFEVHSMRIFFLTRHLSLKDAIDQMTKERVHDYLLRCDKALEKLGVKERRFAVAGLNPHSGENGLFGREEMDEITPGIELAKKDGINAVGPVPADSVFHHALNGRYDAVLSLYHDQGHIAAKMTDFERTISITNGLPFLRTSVDHGTAFDIAGKGIASTVSMEEC... | Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP). |
Q9RC99 | RECF_HALH5 | DNA replication and repair protein RecF | MHIERLTLKQFRNYDELDVSFEPNVNVIIGENAQGKTNVIEAIYFLALAKSHRTARDKELIQWEAPFARIEGAFQKQNGPLSLHVVLSGKGKKVKVNGLEQRRLSDYIGAVNVVMFGPEDLNLVKGSPQIRRRFLDMELGQMSPVYLHQLAMYQKILLQRNHLLKQLFGKANSDPMLDVLTDQLIEVAVEVTKKRFEFIQLLQRWAEEIHQAISRGKEKLVITYEPSVHVSEQLNLSKLREGFYQAYEQKKERERQRGTTLFGPHRDDLVFFVNDKDVQTYGSQGQQRTTALSLKLAEIELMKETVGDYPILLLDDVLSE... | The RecF protein is involved in DNA metabolism it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP (By similarity). |
Q9RCA1 | DPO3B_HALH5 | Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (DNA polymerase III subunit beta) | MHFVIDRDIFVQNVNHVSKAVSSRTTIPILTGIKIVADHEGVTLTGSDSDISIETFIPLEEGDRQNVEVKQEGSIVLQAKVFAEIVKKLPEQEIEIHVQDSFVTTIRSGSSVFNLNGLDPDEYPRLPVLEEDHVFRLPQKILKDIIRQTVFAVSTQETRPVLTGVNFEIEDGILTCTATDSHRLAMRKVPVEKNDDELQFSNVVIPGKSLNELSKILDENEELLDIVVTENQTLFKLKNMLFFSRLLEGKYPVTKNMIPKEAKTSFAVHTKAFLQTLERALLLSREGKNQVINLKTLGDGVVEVTAITPEIGKVTENVAT... | Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalyti... |
Q9RCA2 | DNAA_HALH5 | Chromosomal replication initiator protein DnaA | MENIHDLWERALKSMEKKVSKPSFETWLKQTKANSIEDSTIIITAPNEFARDWLEKHYDELISETIDDLTGVRLYPKFVIPTSQLDEPFVEQELKKPMKQPPAQNGEMPNNMLNDKYTFDTFVIGSGNRFAHAASLAVAEAPAKAYNPLFIYGGVGLGKTHLMHAIGHYVMDHNPNAKVVYLSSEKFTNEFINAIRDNKAVNFRNKYRNVDVLLIDDIQFLAGKEQTQEEFFHTFNALHEDNKQIVISSDRPPKEIPTLEDRLRSRFEWGLITDITPPDLETRIAILRKKAKAENLDIPNEVMLYIANQIDTNIRELEGA... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). |
Q9RCA4 | RNPA_HALH5 | Ribonuclease P protein component (RNase P protein) (RNaseP protein) (EC 3.1.26.5) (Protein C5) | MKKEHRIKRSDEFSRVFNEGFSVANRQFVIYVLPKEGQDFFRVGLSVSKKIGNAVTRNRVKRLIRTFFQEHEQAISGERDYVIIARKPAADMTYEQVKGSLWHVCKKAKIIQPKVRAHK | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the riboz... |
Q9RCA5 | YIDC1_HALH5 | Membrane protein insertase YidC 1 (Foldase YidC 1) (Membrane integrase YidC 1) (Membrane protein YidC 1) | MYRKFGMAAMLVSILLLMTGCFNVNEPINAQSEGIWDSYFVYPLSWLMIYFANAFNGSFGLAIIVVTLLIRLLILPLMIKQLKSTRAMQALQPEMQALREKYSAKDQRTQQKLQQETMALFQKHGVNPLAGCFPVLIQMPILLAFYHAIMRTREIGDEHFLWFVLNQPDPILLPIIAGITTFLQQKMMMVTDNPQMKVLLYVMPVMILVFAMFLPSSLALYWVIGNLFMILQTYFITGPNVGAKKVAADVKVGGKKK | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. {ECO:0000255|HAMAP-Rule:MF_01811}. |
Q9RCA8 | MNMG_HALH5 | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG (Glucose-inhibited division protein A) | MSYQGGEFDVIVVGAGHAGVEAGLAAARMGANTLMLTLNLDAVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNTGKGPAVRALRAQADKFLYQHEMKKTIEEEENLLLRQGMVERLIIEDGECRGVITNTGAEYRAKAVVVTTGTYLRGKIIIGDLAYESGPNNMQPSINLSYHLQELGFEMVRFKTGTPPRVNGETIDYDKTEIQPGDEVPRAFSYETTKYITDQLPCWLTYTGDKTHQIINDNLGRSPMYSGMIEGTGPRYCPSIEDKIVRFNDKPRHQIFLEPEGRHTSEVYVQGLSTSLPEDV... | NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00129}. |
Q9RCE7 | TRPA_VIBME | Tryptophan synthase alpha chain (EC 4.2.1.20) | MDRYQHLFQRLAAHNQGAFVPFVTIGDPNPQQSLRIMQTLVEAGADALELGIPFSDPLADGPTIQGAISALDSGTKPIRCFEADQAPIRAQDIPIYLLMYANLVYARGIDNFYQRCQQAGVDSVLIADVPTNESAEFGPAAKKYAIHPIFIAPPTASDETLQSVAELGSGYTYLLSRSGVTGAETKANMPVHALLERLNQFSAPPRRLGFGISEPEQVKQAIESGAAGAISGSAVVKIIEHHLAKPEAMLAELKTFVSAMKSATKHDK | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. |
Q9RCE8 | TRPB_VIBME | Tryptophan synthase beta chain (EC 4.2.1.20) | MAKLNAYFGEYGGQYVPQILVPALDQLEQAFIDAQEDPDFRAEFMSLLQEYAGRPTALTLTRNLTKGTKTKLYLKREDLLHGGAHKTNEVLGQGLVGKRMGKSAIIAETGAGQHGVGSALASALVGLKCRIIMGAKNLERQSPNVFRMKLMAESIPSSVTLKVAVNEALRDWSATETTHYYLGTAAGPHPYPTIVREFQRIIGEETKLQILAREGRLPDAVLACIGGGSNAIGMFADFIDEANVRLIGIEPAGKGIDTHQHGAPLKHGKTGIFFGMKAPLMQDSYGQVEESYSVSAGLDFPSVGPQHAHLNAIGRANYES... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}. |
Q9RD25 | THIO2_STRCO | Putative thioredoxin 2 (Trx-2) | MTSTVELTKENFDQTVTDNEFVLIDFWAEWCGPCKQFGPVYEKAAEANPDLVFGKVDTEAQPELAQAFGISSIPTLMIVREQVAVFAQPGALPEAALTDVIGQARKLDMDEVRKAVAEQQAQAGQNGQEGQEGQ | Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). |
Q9RDD6 | HRCA_STRCO | Heat-inducible transcription repressor HrcA | MLSERRLKVLRAIVQDYVGTEEPVGSKALTERHNLGVSPATVRNDMAALEDEGFIAQPHTSAGRIPTDKGYRLFVDKLAGVKPMTAPERRAIQNFLEGAVDLDDVVARTVRLLAQLTRQVAVVQYPSLTRSTVRHVELLSLAPARLMLVLITDTGRVEQRMVDCPAPFGEASLADLRARLNSRVAGRRFADVPALVEDLAEPFEAEDRGTVSTVLSTLLETLVEENEERLMIGGTANLTRFGHDFPLVIRPVLEALEEQVVLLKLLGEAKDPGVTVRIGHENAHEGLNSTSVVSVGYGSGGEAVAKLGVVGPTRMDYPGT... | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}. |
Q9RDE9 | GUDD_STRCO | Probable glucarate dehydratase (GDH) (GlucD) (EC 4.2.1.40) | MTRDLTITAVHLTPILVADPPLLNTQGVHQPYTPRLIVEVETADGVTGVGETYGDAKYLELARPFAAKLVGRQVSDLNGLFTLADEVAVDSSRVFGQVDVGGLRGVQTADKLRLSVVSGFEVACLDALGKALGLPVHALLGGKVRDAVEYSAYLFYKWADHPEGVASEKDDWGAAVDPAGVVAQARAFTERYGFTSFKLKGGVFPPEEEIAAVKALAEAFPGHPLRLDPNGAWSVETSLKVAAELGDVLEYLEDPALGTPAMAEVAAKTGVPLATNMCVTTFAEIQEAFTKGAVQVVLSDHHYWGGLRNTQQLAAVCRTF... | Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc). |
Q9RDK1 | PROA_STRCO | Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase) (GSA dehydrogenase) | MTTLSPYDSMSPVTRAAYRAKSAAADLAPLPRAAKDDALLAVADALEVRTSEIVEANAQDVAKARAAGTSEAIVDRLTLTPERVRAIASDVRDVVALPDPVGEIVRGSTLPNGIDLRQVRVPLGVVGIIYEGRPNVTVDAAALCLKSGNAVLLRGSSSAYRSNTALVRVVRDAVGGAGLPADAVQLVPGESRESVRELMRARGLVDVLIPRGGASLISTVVQESTVPVIETGTGNCHVYVDAHADLDMAVDILINSKAQRVGVCNAAETLLVHQDVAAEFLPRALAALAEAGVTVHADERVMAHAKDSGANVVEATPEDW... | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412}. |
Q9RDM3 | RS20_STRCO | Small ribosomal subunit protein bS20 (30S ribosomal protein S20) | MANIKSQIKRNKTNEKARLRNKSVKSSLKTAIRKAREAAAAGDVEKATEFQRVASRELDKAVSKGVIHKNQAANKKSALAQKVGALKG | Binds directly to 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_00500}. |
Q9RDV2 | RL19_MYCGA | Large ribosomal subunit protein bL19 (50S ribosomal protein L19) | MNKLNKQNIINHVNNLQLKKSVPNFQVGDTVSVSIKIADEKRTRIQKFDGLVLRRKGSGLSETFIVRKESSGVGVEKNFHVHNPNIEIELKRKGKVRRAYISYMRERSGKSARIKEKVVNTK | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. {ECO:0000255|HAMAP-Rule:MF_00402}. |
Q9RDV3 | TRMD_MYCGA | tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) | MKIVVLTLFDDFVRSYYDFSIIKNALDKKAVELEVINFRQYANDKHKTVDDTIYGGSAGMLLKLEPLVNCLRDIKQNQFKDPNKIRTYLLSPQGEVYDQNKAVALSQSDHDLILIAGRYEGFDERIYHYVDGALSVGDFVITGGELAALIVVDSIVRLLPNVINKDSLSSESFNNYLLDYPMYTKPYDFEGYKVPDVLLSGNHQAIAAFNQQEAINNTKMKRPDLYLKYKSNLK | Specifically methylates guanosine-37 in various tRNAs. |
Q9RDV7 | RS11_MYCGA | Small ribosomal subunit protein uS11 (30S ribosomal protein S11) | MAKKKKTVASNGIAHIHATSNNSIITITDINGNAITWSSSGAIGYKGAKKKTPYSAGVAAEKAAKEAMAMGLSTIKIYVNGVGRGKETAIRSLAACGLTITEIHDVTPIPHNGCRPPKKPR | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01310}. |
Q9RDV8 | RS13_MYCGA | Small ribosomal subunit protein uS13 (30S ribosomal protein S13) | MARILGIDIPNNKRVEISLTYIYGIGKPRAQEILRKAKIDFNKRVKDLSDEELALIRSVASTYVLEGDLRRDVALNIKRLMEVGSYAGLRHRRGLPVRGQRTKSNARTRKGPRKTVANKKIESK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. {... |
Q9RED7 | RLMB_BURSP | 23S rRNA (guanosine-2'-O-)-methyltransferase RlmB (EC 2.1.1.185) (23S rRNA (guanosine2251 2'-O)-methyltransferase) (23S rRNA Gm2251 2'-O-methyltransferase) | MPRLKLLHGFHAITARLRAFPATVNEVWYDPARQDARMRAFLHLAASANARLIAADASRLNALSGEKRHQGVVARVTEATRAHSLETLLDTIEGQPLLLALDGVTDPHNLGACLRVADGAGAHAVIAPRRRAAGLTAAAAKAANGAAETVPYLTVINLARALRALKNAGIQVIGTADDATTSLFDIQLDGALALVMGAEGAGMRRLTREACDEVVRIPLAGHVQSLNVSVASGICLFEAVRQRLKRL | Specifically methylates the ribose of guanosine 2251 in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}. |
Q9REF2 | HRCA_BRADU | Heat-inducible transcription repressor HrcA | MAHHDPIHLIAPRAGLAQLNERSRDIFRQIVESYLATGEPVGSRNISRLIAMPLSPASVRNVMADLEQLGLIYAPHTSAGRLPTELGLRFFVDALMQVGDLNDAERQSIQSQLTSVGQAQSVEAALDQALTRLSGLTRAAAVVLTPKSNARLKHIEFVRLEPEKALVILVGEDGQVENRVLTLPPGVPSSAITEAGNFLNSRIRGRTLAEARLELETALGEARAELDQLTQKVISAGIASWSGGENEDRQLIVRGHANLLEDLHALEDLERVRLLFDDLETKRGVIDLLGRAETAEGVRIFIGSENKLFSLSGSSTIISP... | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}. |
Q9REF4 | RISB_BARHE | 6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) | MTIEICKKLHVLIVEARFYDGISDALLTGAVSTLQKAEATYDIVTVPGALEIPGAIAFAEKNSKIYYDGYVALGCVIRGETYHFEIVANDSCRALMDLTIHKHLAIGNGILTVENEKQAWARAKQDEKNKGGFAAQAALCMIALKKRFGEIIKYG | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178}. |
Q9REJ6 | RECA_PAEAU | Protein RecA (Recombinase A) | LGIGGLPRGRVVEIYGPESSGKTTVALHAVANAQRAGGIAAFIDAEHALDPDYAAKLGVDTDALLVSQPDTGEQALEIMDMLVGSGSLDIVVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKITGRLSQTKTTAIFINQLREKIGVFFGSPETTTGGKALKFYASVRIDVRRIQTLKEGADSVGNRTKAKIVKNKMAPPFKIAEFDIIYGQGI | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (By similarity). |
Q9REM0 | HYPA_CERSP | Hydrogenase maturation factor HypA | MHEMSLCEGIRGIVEDQARRHGFATVKVLRLEIGRFAGVEKAALGFAFDVVMRGSAAEGARLEILELPGRALCYDCGEEAAIQDRFDPCPLCGGGRLMPVGGDEMRIKDMEVQ | Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. {ECO:0000255|HAMAP-Rule:MF_00213}. |
Q9REM8 | ADP2_MYCGA | Adhesin P1 (Adherence protein A) (Attachment protein) (Cytadhesin P1) | MKKLIFKLSVGITPLALIGLGSFGLAVSGAKPNNLKPVNQVGEMNSQGQSNLLEKARRWRNSNFTSLSIDGTNPGALVLTGSKSISRIDLYGNVIWTFDPGNTNDLTGKVGFYDANNRLTAFSGDVPFNVSDLSSKTVVEATQDQEDPNVFYLLLIPDAAVQQEQKTKDQVFENYFMSDAPATGDTSAEGSATPAGGGSSSSAAGGGAVAPAAASSTARLVEEGNSAGMGTMTPTASTSETVIDYNSDQNKIPKPKTLLDSSESSESINGGRTYANINTQNNLQGVIVKVNENLFNSENPFAVENMAFIKPKDMVDNYPS... | Could be involved in cytadherence. |
Q9REQ2 | DEF_ZYMMO | Peptide deformylase (PDF) (EC 3.5.1.88) (Polypeptide deformylase) | MALLPILEVPDPRLREKSTVVEVFDDNLQRLIDDMFETMYKAPGIGLAAIQVGVAKRLLVIDLQQPEEGGEAKRNPMVFINPELTPEGEEKRLYNEGCLSVPDQYAEVRRPSVINAKWQDRDGNFHEERIEGLLATCLQHEMDHLEGILFIDHLSRLKRGMLMKKLLKERKLREDSY | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. {ECO:0000255|HAMAP-Rule:MF_00163}. |
Q9REQ3 | RMUC_ZYMMO | DNA recombination protein RmuC homolog | MTAFLPFLAFLFGLIIAGLPLLWYIRQQKTALDGLQARVLEGAKAEEQARRIPALEQAVESWREKASLLMAEQAANKRGEEEREKAYRQQIEQLKATEDALSQKFDSLAAKTLEKAHGQFLEQAQMRFAKSEREGEAKLELLLQPVKDSLKRYEASVKEAEQLRQTEYGSLTALVSTMREGQEAVKNEANKLVNALRTAPKARGCWGEQQLRNVLESCGLSEYVDFETEVSVNSEKGRLRPDAIIRIPNGSILVVDSKVSLNAYQDAYDAVDEDKRQLYLQAHSKAIKAHIDGLSQKNYWDQFKEAPDYVIMFIPGEHFL... | Involved in DNA recombination. |
Q9RER2 | SOPB_SALBL | Inositol phosphate phosphatase SopB (EC 3.1.3.-) (Effector protein SopB) | VLTSMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAARTQQQDGLPAKEAHRFAAVAFRDAQVKQLNNQPWQTIKNTLTHNGHHYTNTQLPAAEMKIGAKDIFPSAYEGKGVCSWDTKNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKDPLLRQVGAENKAKEVLTAALFSKPELLNKALAGEAVSLKLVSVGLLTASNIFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGDLQTVKIKPDVAAFNVGVNELALKLGFGLKASDSYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVN... | Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing v... |
Q9REV5 | RECX_AMYMU | Regulatory protein RecX | MPPAELPPEERYKKAKEICFDLLAVRARTQEELRQALRRKGFDEETSETLLGKLDRAGLVNDAEFAELWVKSRHTTQGLSRTALMAELRRKGVDDEVAAQAAGEVDRESEEQMARELVRKRLGSLGNVDEQTALRRLLGFLARKGYPQGLAYTVIKEELREYGAESTLLDDAVID | Modulates RecA activity. |
Q9REV6 | RECA_AMYMU | Protein RecA (Recombinase A) | MPAAPDKDKALELALAQIDKQYGKGSVMRLGEEGRAPIAVIPTGAIALDVALGIGGLPRGRVIEVYGPESSGKTTVALHAVANAQRNGGIAAFIDAEHALDPDYAKKLGVDTDALLVSQPDTGEQALEIADMLVRSGALDILVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKMTGAMNNSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGGEAVGNRTRVKVVKNKMAPPFKQAEFDILYGHGISREGSLIDMGVDQAILRKSGAWYTYEGDQLGQGKENARKFLRDNPDIANEI... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. {ECO:0000255|HAMAP-Ru... |
Q9RF07 | GATA_STAAU | Glutamyl-tRNA(Gln) amidotransferase subunit A (Glu-ADT subunit A) (EC 6.3.5.7) | MSIRYESVENLLTLIKDKKIKPSDVVKDIYDAIEETDPTIKSFLALDKENAIKKAQELDELQAKDQMDGKLFGIPMGIKDNIITNGLETTCASKMLEGFVPIYESTVMEKLHNENAVLIGKLNMDEFAMGGSTETSISKKTVNPFDHKAVPGGSSGGSAAAVAAGLVPFSLGSDTGGSIRQPAAYCGVVGMKPTYGRVSRFGLVAFASSLDQIGPLTRNVKDNAIVLEAISGADANDSTSAPVDDVDFTSEIGKDIKGLKVALPKEYLGEGVADDVKEAVQNAVETLKSLGAVVEEVSLPNTKFGIPSYYVIASSEASSN... | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00120}. |
Q9RF98 | OADB_HAEDU | Oxaloacetate decarboxylase beta chain (EC 7.2.4.2) | MESIIALFQGMGIMHITLGQVIMIIVSLILLWLAIARRFEPLLLLPIGFGGLLSNIPEAGLAMTALDHLLHYAHTEQLTIIAEKVNSSSLDVHTIKQAIAFAPPSVQNELEVIASDLGYNAGILALFYKVAIGYGVAPLIIFMGVGAMTDFGPLLANPRTLLLGAAAQFGIFTTVLGALGLNWLGIIDFSLPQAAAIGIIGGADGPTAIYLASKLAPELLGAIAVAAYSYMALVPLIQPPIMKALTTEQERKIRMVQLRTVSAREKIVFPIVLLLLVALLLPDAAPLLGMFCFGNLMRASGVVERLNETAQNALINIVTI... | Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. |
Q9RFA0 | OADG_HAEDU | Oxaloacetate decarboxylase gamma chain (EC 7.2.4.2) | MTNAELFGEGINLMIAGMGFVMFFLIILIYAISVISRLINKYFPDPTQTPPAQPIPAVIPPTDLERLRPVIVAAIAHHRRQQRSN | Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. |
Q9RFJ6 | ROT_STAA8 | HTH-type transcriptional regulator rot (Repressor of toxins) | MHKLAHTSFGIVGMFVNTCIVAKYVIINWEMFSMKKVNNDTVFGILQLETLLGDINSIFSEIESEYKMSREEILILLTLWQKGSMTLKEMDRFVEVKPYKRTRTYNNLVELEWIYKERPVDDERTVIIHFNEKLQQEKVELLNFISDAIASRATAMQNSLNAIIAV | Global regulator with both positive and negative effects that mediates modulation of several genes involved in virulence. Negatively regulates the transcription of several known virulence factors such as lipase (geh), hemolysins (hla and hlb) and proteases (splA through splF, sspB and sspC). Positively regulates the ex... |
Q9RFV8 | NQRD_VIBC1 | Na(+)-translocating NADH-quinone reductase subunit D (Na(+)-NQR subunit D) (Na(+)-translocating NQR subunit D) (EC 7.2.1.1) (NQR complex subunit D) (NQR-1 subunit D) | MSSAQNIKKSIMAPVLDNNPIALQVLGVCSALAVTTKLETAFVMTLAVTFVTALSNFSVSLIRNHIPNSVRIIVQMAIIASLVIVVDQVLKAYLYDISKQLSVFVGLIITNCIVMGRAEAFAMKSAPVPSLIDGIGNGLGYGFVLITVGFFRELFGSGKLFGMEVLPLVSNGGWYQPNGLMLLAPSAFFLIGFLIWVIRILKPEQVEAKE | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00428}. |
Q9RFW1 | NQRA_VIBC1 | Na(+)-translocating NADH-quinone reductase subunit A (Na(+)-NQR subunit A) (Na(+)-translocating NQR subunit A) (EC 7.2.1.1) (NQR complex subunit A) (NQR-1 subunit A) | MITIKKGLALPIAGAPSQVINDGKTIKKVALLGEEYVGMRPTMHVRVGDEVKKAQVLFEDKKNPGVKFTAPAAGKVIEINRGAKRVLQSVVIEVAGEEQVTFDKFEAAQLAGLDREVIKTQLVESGLWTALRTRPFSKVPAIESATKAIFVTAMDTNPLAAQPELIITEQQEAFVAGLDILSALTEGKVYVCKSGTSLPSSSQSNVEEHVFDGPHPAGLAGTHMHFLYPVNAENVAWSINYQDVIAFGQLFLTGELYTDRVVSLAGPVVNNPRLLRTVVGASLEDLTDSELMPGEVRVISGSVLSGTQASGPHAYLGRYH... | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00425}. |
Q9RGG2 | PTRD_LACCA | PTS system sorbose-specific EIID component (EIID-Sor) (Sorbose permease IID component) | MADQPVQVNKLKTKITKGDMFKTFVFENFQQASFNFERIHALAFCVDMIPTIKRVYSKKEDQVAALKRHLVFFNTTPAMCGPIVGVTMALEEGRAAGEPIDDGTINSFKVGLMGPLAGVGDPLMWGTLRPILAALGASLALQGSWLGPILFFVAFNAVRLSLKWYGLQLGFSRGLALVKDMSGNLLQKITEGATVLGLFIMGILVTKWTTINVPLVVSKTTVNGKTTVTTLQNILDQFCPGLLALGWTLLCMYLLRKKVSPILLIFALFGVGIVGYWLGILK | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II SorABCD PTS system is involved in L-sorbose transport. |
Q9RGG3 | PTRC_LACCA | PTS system sorbose-specific EIIC component (EIIC-Sor) (Sorbose permease IIC component) | MAISTIQIILIFIWSSVVGMGSVLDEFQTHRPLIACSIMGLILGDPKTGIILGGTLELIALGWMNIGAAQSPDSALASTISTILVIVGNQDIQKGIAIALPVAAAGQVLTVLARTVTVAFQHAADREAEKANFTAIIWLHFTALIVQALRVSIPTTIVAVFVSPEEIKSMLDALPEVITGGLAVAGGFIVVVGYAMILNMMSVKYLMPFFYQGFVLGGYLKLSLLAWGAVGLIFAIVYVQLNPKFATNHNNGTGGSGGTVAAAGDHPAALPEDELDD | The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II SorABCD PTS system is involved in L-sorbose transport. |
Q9RGM3 | MDCB_ACICA | Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase (2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase) (EC 2.4.2.52) | MQTVQKHDHLFLDISQHAMRLDLLARTALYEEVSLAHKPGLVCPTTQGSHQDMDFALFERSIQSLTYYFQEQCLNGYHEVSFDSIRQCGIQAEQDMMAATKQINTHKGAIFNLGFASAAVGKCFAQDILLNAISISRMIQQTWQEELLHHLERNPNSHGQRMRSQYGITGAIEEVASGFKTVLDVAVPHYLEIYAKTGDKKRASLQALFALMSHLQDTNIVWRGGLSALYIVQDMAKQFLARGGVLQHNWMQDVSKVEDYFVRHHLSPGGSADLLGVTLFMLKVEHEFRNII | Involved in the formation of 2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A, the prosthetic group of the acyl-carrier protein of the malonate decarboxylase. |
Q9RGW9 | MECA_LISMO | Adapter protein MecA | MEIERINEDTIKFYISYLDLEERGFNQEDVWYDREKSEELFWDMMDELKYEEEFSPEGPLWIQVQALKHGLEVFVTKATIGGKGEDGFDVTLSSPDELAEEKIEKLLEENFNPVKKEALGEDDTLEFILEFRDFEDAISLSRATGLENLVTKLYSYQGKYYLNVEFPENKYDESNIDNAVSILLEYGLESNLTGYMLAEYGKVIFDVPALKQIRKHF | Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. {ECO:0000255|HAMAP-Rule:MF_01124}. |
Q9RGX0 | SPX_LISMO | Global transcriptional regulator Spx | MVTLYTSPSCTSCRKARAWLEEHDIPYKERNIFSEPLSLDEIKEILRMTEDGTDEIISTRSKTFQKLNVDLDSLPLQQLFELIQKNPGLLRRPIIIDEKRLQVGYNEDEIRRFLPRRVRTYQLREAQKMVN | Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes. Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP). This interaction can enhance binding of RNAP to the promoter region of target genes and ... |
Q9RH04 | HIS1_ZYMMO | ATP phosphoribosyltransferase (ATP-PRT) (ATP-PRTase) (EC 2.4.2.17) | MTKPLVFAIPKGRILKEALPMLEAAGIIPEPAFLDKESRLLRFKTNRPDIEIIRVRAFDVATFVAHGAAQMGIVGSDVIEEFSYPELYAPVDLDIGHCRLSIAEPKRLAKDDDPREWSHVRVATKYPHLTHRHFEARGVQAECIKLNGAMEIAPALGLAGRIVDLVSSGRTLEENGLVEVEKIMPISARLIVNRAAFKMRAGDIAPLVENFRRLVGVADNVA | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). |
Q9RH11 | RPPH_ZYMMO | RNA pyrophosphohydrolase (EC 3.6.1.-) ((Di)nucleoside polyphosphate hydrolase) | MDNLEYRSGVGIMLLNKDNLVFAACRNDMKEEAWQMPQGGLEAKETPEVGVLRELEEETGIPPRMVAIISHTKEWLTYDFPADLQASFFKNKYRGQRQLWFLARYLGRDEDININTDKPEFRAWKWVEPKQLPDLIVAFKKPLYEKILSEFSASL | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. {ECO:0000255|HAMAP-Rule:MF_00298}. |
Q9RH31 | GVPA_ANCAQ | Gas vesicle protein A (GvpA) | MAVEKINASSSLAEVVDRILDKGVVVDAWVRVSLVGIELLAVEARVVVAGVDTYLKYAEAVGLTASAQAA | Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell. {ECO:0000255|HAMAP-Rule:MF_00576}. |
Q9RH43 | RPOB_RICMA | DNA-directed RNA polymerase subunit beta (RNAP subunit beta) (EC 2.7.7.6) (RNA polymerase subunit beta) (Transcriptase subunit beta) | MVSLRDNIEAQPLSHNRRIRKNFGHINLVADIPNLIEIQKNSYEKNFLQLNIKDSERKNKGLQSILNSIFPISDSSNIANLEFVKYEFDTPKYDVEECSQRSLSYAAPLKVTLRLSIWDIDEDTGTREIKGIKEQEVYMGDIPLMTKNGTFIINGTERVVVSQMHRSPGVFFYHDEGKVHSSGKLLYSARVIPYRGSWLDLEFDAKDVIYFRIDRKRKLYITTLLRAIGMSTEEIIKFYYNSVTYKLVKNKGWAVKFIPQHITAHRLTSDLVDADTGNILLKAGQKITPRLAKKYFGEGLNNILVAHETLIGKYLSEDLR... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_01321}. |
Q9RH67 | RECO_BRADU | DNA repair protein RecO (Recombination protein O) | MEWTDEGIVLGVRRHGESSAIVELLTRAHGRHLGLVRGGAGSRMRPLLQPGNSVSAVWRARLDEHLGTYAVEGLKLRAATLLASSHGVYGVTHLASIARLLPERDPHEEIFGLLEHSLDDFDDIGSAAVHVIHFELAMLAELGFGLALDNCAVTGETTDLIYVSPKSGGAVSRGAGEPWRDRLLRLPPFLRHGETATELTDQDLQDGFRLTGLFLLRHVLEPRGQVHSDARAGFINALTRQQARAAIPAP | Involved in DNA repair and RecF pathway recombination. |
Q9RH74 | SSRP_BRADU | SsrA-binding protein (Small protein B) | MADKNERPIKVMAENRKARFNYAIEDTIEAGIALTGTEVKSIRNGKSTIAESYADSKNGEIWLINATIPEYLQGNRFNHEPKRPRKLLLHRRQINKLIGAVDREGMTLIPLKLYFNERGRAKLQLAVAKGKKLHDKRETEKKRDWSREKGRLLRARG | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene the 2 termini fold to resembl... |
Q9RHG2 | ARAA_MYCSM | L-arabinose isomerase (EC 5.3.1.4) | MAEHFTDEEIWFVTGSQSLYGQEILDQVAEQSRALAERLDASADLPVAVRWKPVVTTSEAILDVLRDASSSPQCVGVITWMHTFSPAKMWIRGLSALQKPMLHLHTQFGVEIPWDTIDMDFMNLNQAAHGDREFGYIQTRLSVPRTTVAGHVGDPRTTARIGSWMRAALGAAELRSLRIARFGDNMRDVAVTEGDKVEAESHFGVSVNTYSVNDLAKAVYDVSDPEIDKLVQEYEDTYAVAEELRRGGERHASLREGARIELGLRHFLADGFGAFTTNFEDLGDLRQLPGLAVQRLMADGFGFGAEGDWKTSAMVRTVKT... | Catalyzes the conversion of L-arabinose to L-ribulose. {ECO:0000255|HAMAP-Rule:MF_00519}. |
Q9RHM3 | UREE_CORGL | Urease accessory protein UreE | MIITAIDTNIYDQPEFVEGRDVIGVRFEDLVLDKRIQRVALPGGEELGLRLNHGHPILREGDVLKADDKTVFVVEIIPTDVLVITPSDIHQMGFVAHSLGNRHLPAQFSKPGELTEKAAMIVQYDHTVVSFLDEHGIEYQRTELVPPIPFRHSGHTH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. {ECO:0000255|HAMAP-Rule:MF_00822}. |
Q9RHV8 | DSBA_BURCE | Thiol:disulfide interchange protein DsbA | MKKLLSTLLLSLGLAAGLAQASPAAPASGKDFEVMKSPQPVSAPAGKVEVIEFFWYGCPHCYEFEPTIEAWVKKQGNNIDFKRVPVAFRDDFLPHSKLFYAVSALGISEKVTPAIFNAIHKQKNYLLTPQAQADFLATQGVDKKKFMDAYNSFSVQGEVNQSAKLLKDYAIDGVPTVVVQGKYKTGPAYTNSIPGTAQVLDFLVKQVQDKKL | Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance. |
Q9RJ20 | COBQ_STRCO | Cobyric acid synthase | MNGGLLVAGTTSDAGKSVVTAGICRWLVRQGVKVAPFKAQNMSLNSFVTRDGAEIGRAQAMQAQACRVEPTAHMNPVLLKPGGERSSQVVLLGRPVGEMSARGYHGGRQERLLGTVLDSLAELRGTYDAVICEGAGSPAEINLRRTDIVNMGIARGAGLPVLVVGDIDRGGVFASFFGTVALLAPEDQALVAGFLVNKFRGDVSLLEPGLDMLHGLTGRRTYGVLPFRHGLGIDEEDGLRVSLRGTVRESVVAPPVGEDVLRVAVCAVPLMSNFTDVDALAAEPGVVVRFVDRPEELADADLVIVPGTRGTVRALEWLRE... | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. {ECO:0000255|HAMAP-Rule:MF_00028}. |
Q9RJ68 | TATA_STRCO | Sec-independent protein translocase protein TatA | MFGRLGAPEIILILVVIILLFGAKKLPDMARSLGKSARILKSEAKAMKSEAKADDAAPADPPNPEQSAAQRTIQAAPGDVTSSRPVTEPTDTTKR | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. {ECO:0000255|HAMAP-Rule:MF_00236}. |
Q9RJ79 | EX53_STRCO | 5'-3' exonuclease (EC 3.1.11.-) | MLLDTASLYFRAYFGVPDSVKAPDGTPVNAVRGLLDFIDRLVKDHRPEHLVACMDADWRPHWRVELIPSYKAHRVAEERPAGPDAEEVPDTLSPQVPVIEAVLDALGIARVGVAGYEADDVIGTYTARATGPVDIVTGDRDLYQLVDDARGVRVLYPVKGVGTLNLVDEAALREKYGVDGAGYADLALLRGDPSDGLPGVPGIGEKTAAKLLAEFGDLAGIQAAVDDPKARLTPTQRKRLTEAGPYLAVAPKVVRVAADVPLPDTGTALPHGPRDAAALEALAARWGLGGSLQRLLTTLTA | 5'-3' exonuclease acting preferentially on double-stranded DNA. |
Q9RJA9 | GVPJ2_STRCO | Probable gas vesicle protein J2 (GvpJ2) | MTDLDHRYPGEETEPYGPPSGSLADLLERVLDKGIVIAGDIKIDLLDIELLTIRLRLFIASVDTAKKAGIDWWETDPALSSRAARDALAEENARLRERLDALEGAAGETTGAVR | A minor component of the gas vesicle, might be involved in nucleating gas vesicle formation (By similarity). Gas vesicles (GV) are hollow, gas filled proteinaceous nanostructures. It is not clear what function GVs perform in soil bacteria (Probable). |
Q9RJB4 | GVPA2_STRCO | Gas vesicle protein A2 (GvpA2) | MITYDDEVVCAPRAGTLYDVLELILDRGMVIDVFVRVSLVGIEILKVDARIVVASVDTYLRFAEACNRLDLEHDVRSKTVPEMFGSPMAKTVGRAGARRTARSLTDKVRDVLTPEHEHEEEPEEAEDRPRAGAERGRSTQRPRSRPAARPRDEDDRPRSRPRRRTEEEDR | Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell (By similarity). It is not clear what function GVs perform in soil bacteria ... |
Q9RK00 | XYLB_STRCO | Xylulose kinase (Xylulokinase) (EC 2.7.1.17) | MSAAEGPLVVGVDTSTQSTKALVVDAATGRVVASGQAPHTVSSGTGRESDPRQWWDALGEALSQCGEAAREAAAVSVGGQQHGLVTLDARGEPVRPALLWNDVRSAPQARRLIDELGGAKAWAERTGSVPSASFTVTKWAWLTEHEPEAARAVKAVRLPHDYLTERLTGEGTTDRGDVSGTGWWASGTEAYDEEILARVALDPALLPRVVRPGEVAGTVRDGHGLPFSKGTLVAAGTGDNAAAALGLGLRPGVPVMSLGTSGTAYAVSQRRPADPTGTVAGFADARGDWLPLACTLNCTLAVDRVASLLGLDREAVEPGT... | Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02220}. |
Q9RK61 | ACP_STRCO | Acyl carrier protein (ACP) | MPSTADERQLLDELRDLLAATVEDLTVEEIGPDSSLQDDLGVDSLARLELVAAIEDRWQIEVPQEQADRLTTVRQIAAHLAEAVAAPAGGTA | Carrier of the growing fatty acid chain in fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. |
Q9RKC6 | Y3161_STRCO | Putative ABC transporter ATP-binding protein SCO3161 (EC 7.-.-.-) | MTGPAAAPVPDAPASLDVSGLAFAYPDGHQALFGVDFCVARGERVALLGPNGAGKTTLVLHLNGILTGGTGTVTVAGLPVDKRNMAEIRRRVGIVFQDPDDQLFMPTVREDVAFGPAAAGVKGAELEACVDRALTLVGMAEFKDRPPHHLSFGQRRRVAVATVLAMEPEILVLDEPSSNLDPASRRELADILRSLDVTVLMVTHDLPYALELCPRALILSDGAIAADGPTAALLSDDDLMRAHRLELPFGFDPRSVRASG | Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). |
Q9RKQ4 | HMUV_STRCO | Hemin import ATP-binding protein HmuV (EC 7.6.2.-) | MRGVKLPRLVPSRPVPPPPAAPGEVLAAAGGLRVHLGGRPVLDGVDVEVRAGEVLALVGPNGAGKSTLLGALAADVPAAEGVVRVHGRPVSDWSAPELALRRAVLPQSASLSFPFAVEEVVRMGRAPWAGGDRADEDEAAVAEAMARTEVAGFAGRPFSALSGGERARVALARVLAQRAPLLLLDEPTAALDLRHQELVLRLCRERARAGDAVVVVLHDLALAAAYADRVALLRSGRIAAGGPPSEVFAQGLLSEVYDQPVEVFPHPRTGALLVVPHRSP | Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01718}. |
Q9RL17 | BVMO1_STRCO | Baeyer-Villiger monooxygenase (BVMO) (EC 1.14.13.-) | MAHAQELTPEALAGLRERYRRERERRVRPDGTRQYLGADAEFGFYAADPWAGESDVREPVRDRVDVAVVGGGFGGVLAGARLRQQGVARVRVVEKGGDFGGTWYWNRYPGIHCDIEAHVYLPMLDETGYVPEWKYAPGEEIRRHAMRIAETFDLYTDVLFSTAVTSLSWDDTTGEWIVETDRHDAFRATYVITATGVLSELKLPGIPGIERFKGHTFHTSRWDYAYTGGGPDGGLTGLADKRVGVVGTGATGVQVIPKLAEDAGQLHVFQRTPSSVDVRANRRTTARDVGADRAGWASERRDNFLRVVSGEAVEEDLVAD... | Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH and/or NADH as an electron donor. Thus, can convert bicyclo[3.2.0]hept-2-en-6-one into the oxidative lactone products 2-oxabicyc... |
Q9RL45 | PXPA_STRCO | 5-oxoprolinase subunit A (5-OPase subunit A) (EC 3.5.2.9) (5-oxoprolinase (ATP-hydrolyzing) subunit A) | MIDLNADLGEGFGRWTLTDDDALLSVVTSANVACGFHAGDPSVMRRVCDLAAERGVRIGAQVSYRDLAGFGRRAMDVPSDELAAEVAYQIGALRVFAEAAGAPVAYVKPHGALYNRTVHDEGQARAVVAGVRLAGGALPVLGLPGSRLLTAAAEAGLTGVPEAFADRAYTAEGSLVPRSEAGSVVTDEDAVVRRALAFAVEGSVEAVDGTAVAVAARSLCVHGDTPNAARIAARVREALETAGVGIGAFA | Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00691}. |
Q9RL48 | PCP_STRCO | Pyrrolidone-carboxylate peptidase (EC 3.4.19.3) (5-oxoprolyl-peptidase) (Pyroglutamyl-peptidase I) (PGP-I) (Pyrase) | MTRVLITGFAPFGGERVNPSWQAASLVAAEPPAGLAVTAAELPCVFGESLDALRDAIRADNPDLVLCLGQAGGRPGVTVERVGINVDDARIPDNAGGQPIDEPVVPDGPAAYFSTLPVKACVAAMREAGVPAAVSNTAGTFVCNHVAYGLGHLIATEFPHLRGGFAHVPWAPEQVPDGTAPALPPATVAHGLRALLAAAARTPAEQDLKVTEGATH | Removes 5-oxoproline from various penultimate amino acid residues except L-proline. |
Q9RLA0 | DPO1_RICTY | DNA polymerase I (POL I) (EC 2.7.7.7) | MTKKNTLLLIDGYGFVFRAYYAQQSLSSAKGEPVGALYGFTSMLLKLLSDFKPQYGAIVFDSGGKNFRHKIYQNYKANRPTPPEDLIGQLPLIRDVASHLNFAILEKNGYEADDIIATFATKTITLGKEVIIISSDKDLLQLMSKNIKIYDPIKCKYITEDDVIIKFGTTPDKLREVMALIGDRSDNIPGVPSIGPKTASSLITQFGSVENIFNSLDQISSIKQRKTLQNSREAALISWRLIGLDSNVDLDFNLNNLEWSHPNSEKLIGFLQKYGFKSLYKRVENLFYIKINDHEEIVDNKVTEAKEISNASELENFAKE... | In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. |
Q9RLB6 | DPO1_RICHE | DNA polymerase I (POL I) (EC 2.7.7.7) | MTQKNTLLLIDGYGFVFRAYYAQQPLTSPKGEPVGALYGFTSMLLKLLSDFKPKHVAVVFDSGGKNFRHYIYPEYKANRPPPPEDLIVQLPLVRDVASNLNFPILEKNGYEADDIIATFATKTAALGENVVIISSDKDLLQLMSENIKIYDPLRGKYITEDDVVKKFGTTSDKLREVMALIGDRSDNIPGVPSIGPKTASSLITQFGSVENIFNSLDQVSSVKQRETLQNSREAALISWQLIGLDSNVDLDFQLNNLEWSPPNSDKLTGFLQEYGFRSLYKRAENLFDIKINDHKDIVDNKVTEIKEISNKLELENFAKD... | In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. |
Q9RLM3 | T2D1_NEIMC | Type II restriction enzyme NmeDI (R.NmeDI) (EC 3.1.21.4) (Endonuclease NmeDI) (Type-2 restriction enzyme NmeDI) | MSGQKLTAANLVSAIDSLKKNVNYNYVNSSNTHTIQIVHVEKPEGPIKIKRGDTETSISKQAIWRLADALSTGEPVNVDRVFGASYNFRSALEALLAHTPEIYWCKLQRIQPGLNKSEVVEGHKHIIWLPDRPHEKGVMKEYETDVVISEIPSNNVVYDALSLPSTHSEIDIDVKRRHVQIQIALSAIGFQLGFRTWIARNDQGISYGDKKIADLDGIVQKIESEKLISSFDGAVQAAMNIDCIWFRNGKLMPAVMEVEHSTGVRSGLARMKQLKDLLPPYANTRWVIVAPDEDRDKVFKEANVPMFKNLDTQYFPYSAV... | A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-N(12)RCCGGYN(12)-3' and cleaves on both sides of the recognition sequence. |
Q9RLM4 | MTD1_NEIMC | Type II methyltransferase M.NmeDI (M.NmeDI) (EC 2.1.1.37) (Cytosine-specific methyltransferase NmeDIP) (Probable modification methylase NmeDIP) | MMSLKIQPAVPKKSDKPSATNRDCQNFKREKNNLPFQLTDKSCNLDISIRQERKKTLIFSFFSGAGFLDLGFELSGFDIAFVNEVHPPFLEAYKYSRSRMDIPKPKYGYFKGSIDECLYAEKAKDLAGWVKKEKQNGIIVGFIGGPPCPDFSIAGKNKGKDGENGKLSQSYVDLICKNQPDFFVFENVKGLYRTAKHREFFNALKRQLSDFGYVCTEKLINAIEYGVPQDRERIILVGFLSQHVDALQKFDWDAHISFPDALEKDWPTTEEVGRVVSQPANIYPELTVQYWFNRNGVDTHPNASKHFQPRAGLEKFQTIS... | A methylase that recognizes the double-stranded sequence 5'-RCCGGB-3', methylates C-2 on both strands, and protects the DNA from cleavage by the NmeDI endonuclease. |
Q9RLM5 | VSN1_NEIMC | Type II nicking enzyme V.NmeDIP (V.NmeDIP) (EC 3.1.-.-) (NmeDIP very short patch repair endonuclease) | MDRLTPEQRKKCMQSNKSKGTKPELALAKAMWALGLRYRKNSGSIFGKPDFSFKKYKVAVFVDGEFWHGKDWEQRKAEIKGNREFWIAKIERNIRRDMEVTGRLKVEGWAVLRFWSNDVVKNTTCCAEKVRQAVRDKQGLSKFQTREK | May nick NmeDI sequences that contain T/G mispairs resulting from m5C-deamination. If unrepaired, these mismatches can lead to C-to-T transition mutations. The very short patch (VSP) repair process counteracts the mutagenic process by repairing the mismatches in favor of the G-containing strand. This enzyme is an endon... |
Q9RLT6 | CITD_WEIPA | Citrate lyase acyl carrier protein (Citrate lyase gamma chain) | MEIRKSAVAGTLESSDVQIMLSAGNNGIEFELVSDVAKQFGDAIKETITDVLNTYGVTDAAVSVVDKGALDMVIRARAIAVVQRALDIVDTPNWEVL | Covalent carrier of the coenzyme of citrate lyase. |
Q9RM66 | USPC_SALTY | Universal stress protein C | MSYTHILVAVAVTPESHQLLAKAVSIARPVQAKVSLITLASDPELYNQFAAPMMEDLRAVMHEETENFLKMLGEKADYPIEQTFIASGELSQHILAVCRKHHVDLVICGNHNHSFFSRASCSAKSVVSASQVDVLLVPLAGD | Required for resistance to DNA-damaging agents. |
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