entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
B3WEQ9 | HRCA_LACCB | Heat-inducible transcription repressor HrcA | MLTKRQLLVLKEIIRLFTESGQPVGSKTLMQELPVHVSSATIRNDMAALEDAGLITKTHSSSGRVPSTQGYRYYLDHLVEPVRVSRHDLATIKQELGQRYSKMDEIVAQSVQILSNLTSYTAISLGPEVNNIKLTGFRLVPLGNHQVMAILVTNNGNVENQVFTVPPSISSDELEKAIRIVNDQLVGLPLVQVAQRLRTDVPSMLMQYLTSPDGFLDIFGNVLKSAASERFYVGGRLNLMDYLGDSDIHELKKIMSLIDADHGDLTELLGGPIRQTPVQVRLGPELKPIDLANLSLITASYDVGGHGTGMIALLGPTQMP... | 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}. |
B3WEU6 | Y1817_LACCB | UPF0122 protein LCABL_18170 | MEIEKNYRMNSLFEFYGPLLTDKQHAYLALYYGDDYSLGEIATEFNVSRQAVYDNIRRTEASLEEYEKKLHLFANYQAQNEAVDTLVSYARTHYPDDKALSTLLERVADQTAK | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}. |
B4E7D4 | YIDD_BURCJ | Putative membrane protein insertion efficiency factor | MKTVLIALLRFYKVAVSPMLGNRCRFYPSCSDYAREAIQYHGAARGTYLAVRRVCRCHPFSAGGIDLVPPPNSDTRARGEADARSHRL | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B4EDW1 | FETP_BURCJ | Probable Fe(2+)-trafficking protein | MARMIQCAKLGKEAEGLDFPPLPGELGKRIYESVSKEAWQGWLKQQTMLINENRLNMADPRARQYLMKQTEKYFFGDGADQASGYVPPTEG | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B4EUQ7 | FETP_PROMH | Probable Fe(2+)-trafficking protein | MSRTIFCTFLNKEADGLDFQLYPGELGKRIFNEISKEAWGQWMAKQTMLINEKKLNTMNPDDRKLLEQEMVRFLFEGHDVHIDGYTPPEK | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B4F0S1 | FDHE_PROMH | Protein FdhE homolog | MSIRIVPKEQLGKEPSEKSISFIPPVLFPNLKNLYQRRAERFQALAKDNPFADYLEFAAEIALAQEKALHDNPLELDLTPLLSQQTGIAPLDKKTFKRSKHWHALLASIIAELQSVVPESAKIALENLSKASETELEEMATALLNDEYSKVSADKSVFIWAALSLYWAQLAANIPGKAKTEYGENRQFCPVCNSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRIKCTNCELTGKLNYWSLDSENAPVKAESCGDCGSYLKILYQEKDANVDAVADDLASLILDAKMEEEGFARSSINPLLFPNE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B4F0U2 | YIDD_PROMH | Putative membrane protein insertion efficiency factor | MASSLSLGSKILILLIRGYQLGISPLLGPRCRFNPTCSHYGIEALRRFGMIKGSWLTVKRILKCHPLHEGGDDPVPPRKNDDNREN | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B4GH42 | SMG8_DROPE | Nonsense-mediated mRNA decay factor SMG8 (Protein smg-8 homolog) | MGLKDYYTWTFPNIPEHVAQELDQLGRSLVVVGVIGRSRCVLANKMRAFGMEPPVDHEPTDGQLQCYYKPGSSTLLLHFETTFDDAILGQQIDETMEQDGAPFDFDGFYERMKCRFVRMMLLALHVCHILVYVETGQTFDLSLVTIFQLMKFAREQHLMQFLPSLLKETPAGRLLGEKCRLCTPRILFLFENFTHEEGKTRECVSACEFQTEDSIYELLRHHQIITNSSSSSLLALPNNKQFVFYNAHDQLHADRLLQSIEFLNLDMRKLDVKEEEDDLEVLELAPFDGFVKSFGESFESTNYEEQQYKTEHTAWHFLQR... | Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity). |
B4HND9 | WDR48_DROSE | WD repeat-containing protein 48 homolog | MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRIMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWK... | Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). |
B4HWV2 | SMG8_DROSE | Nonsense-mediated mRNA decay factor SMG8 (Protein smg-8 homolog) | MLDDYYTWTYPDIPENVAQELLQLNGSLVVVGVVGRSDCDLANKMLAFGMEPPDDHTPEDGQIQCYYKPGTFSLLLHFESTYDAEISGQMIDVCIEDVDTPFDIDSFFERIRCRFVRMMLLALHVCHIVVWAKFAREQHLMQFLPQMLRETPAARISERTRLCAPRILFLFENFPGDEPKTRESVSTCEFQMEDCIYELLRRYNIVTNSSSNSLVALPNNKQFVFFNAHEELRDDKLLKAIDCLNETMYKPDLKEEEEDLEILAMAPFDGFVKPFTMPVYEKEWENLQYQEDHTVWNFLQRHVHDALVGCFDAGSFKQHA... | Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity). |
B4J8H6 | WDR48_DROGR | WD repeat-containing protein 48 homolog | MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDPNNGKLYSAGRDAIIRVWNTRTESNEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAHKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCIQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEIRNPSNKMLVCEEKAPVLSLGYNIDKTGVWATTWNSDIRCWK... | Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). |
B4JTS9 | SOTI_DROGR | Male-specific protein scotti | MEQGVIEELIHLQLPEMEVANVVNVRDGNGNGNDIDGGNEVWAQHQLDNVNNRQMAILLDAPPEPPIVLHQLPQPVNVPQRLRKKRCFWTITKHFHAQPERCALLSNAWQAVQYVQPAQRSEHFANYMYKHMNSRNYPNGEGLPNRWGHF | Post-meiotically transcribed gene that has a role in late spermiogenesis required for actin cone progression during spermatid individualization. |
B4K843 | SOTI_DROMO | Male-specific protein scotti | MENRVADELIHLPLPEVQAVNVINVRHGDGDGDGENGWERHLDDEQMQAMRLENPQVAMLLDAPHEPPIELHHMLEPVNVPERPRKKRSFLTISKPFHVQPERCALISNGWRAVQCVQPEKRGECFANYLIKHMNSRNYPNGEGLPKRWGQY | Post-meiotically transcribed gene that has a role in late spermiogenesis required for actin cone progression during spermatid individualization. |
B4KRQ4 | WDR48_DROMO | WD repeat-containing protein 48 homolog | MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDSNNGKLYSAGRDAIIRVWNTRTEANEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAHKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCIQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKMLVCEEKAPVLSLGYNIDKTGVWATTWNSDIRCWK... | Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). |
B4LS82 | SMG8_DROVI | Nonsense-mediated mRNA decay factor SMG8 (Protein smg-8 homolog) | MSYKNYYTWKYPDIPEHVAPLLLELQNSLVIVGIIGRSKCAQANKMSAFGMQPDKTHEPADGQILCYYKPGTNMLLLHFETTHDEAVLGQQLLKQTSVDFDSFYEQMRSRFLRMLLLALHVCHILVYVETAQTFDTTLVTICQLLKYVREKHVLDFLPQMLRETAAGSLLSDRARLCTPRVLFLFENYPQDEEKSRERISAYEFQTEDKIYELLRQYNIVTNNANNSLFALPNNKQFVFYNAHEKLRPDQLLLAIEALNATMYKSDSKEEEEDTEILELAPFEGFVKPYGAGYEARESDEQLYRKKHTVWHFLQRHVQDA... | Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity). |
B4LY66 | SOTI_DROVI | Male-specific protein scotti | MEQGVVEELIHLQLPEVEAVDVVNVPDGNGDGDGDGDGDGNDAWERQLDEVQMQAMRLENPQVAMLLDAPHEPPIELHHMLEPVNVPQRPRKKRSFLTISKPFHVQPERCALISNGWRAVQCVQPEKRGEYFANYLIKHMNSRNYPNGEGLPNRWGQF | Post-meiotically transcribed gene that has a role in late spermiogenesis required for actin cone progression during spermatid individualization. |
B4MFM2 | WDR48_DROVI | WD repeat-containing protein 48 homolog | MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDSNNGKLYSAGRDAIIRVWNTRTESNDKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAHKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCIQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKMLVCEEKAPVLSLGYNIDKTGVWATTWNSDIRCWK... | Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). |
B4P7H8 | WDR48_DROYA | WD repeat-containing protein 48 homolog | MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIVSGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWK... | Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). |
B4Q9T2 | SMG8_DROSI | Nonsense-mediated mRNA decay factor SMG8 (Protein smg-8 homolog) | MLDDYYTWTYPDIPENVAQELLQLNGSLVVVGVVGRSDCDLANKMLAFGMEPPDDHTPEDGQIQCYYKPGTFSLLLHFESTYDAEISGQMIDVCIEDVDTPFDIDSFFERIRCRFVRMMLLALHVCHIVVYVENGLTFDPTLLTVFQLAKFAREQHLMQFLPQMLRETPAARISERTRLCAPRILFLFENFPGDEPKTRESVSTCEFQMEDCIYELLGRYNIVTNSSSNSLVALPNNKQFVFFNAHEELRDDKLLKAIDCLNETMYKPDLKEEEEDLEILAMAPFDGFVKPFTMPVYEKEWENLQYQEDHTVWNFLQRHV... | Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity). |
B4QB64 | WDR48_DROSI | WD repeat-containing protein 48 homolog | MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRIMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWK... | Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). |
B4RE94 | YIDD_PHEZH | Putative membrane protein insertion efficiency factor | MNLYESCVRGALRAYKLTLSPLIGRQCRFFPTCSEYAAEALIGHGPVRGSWLTVRRLCRCHPWGPSGWDPPPPPRRKGAKWTCET | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B4RJJ4 | YIDD_NEIG2 | Putative membrane protein insertion efficiency factor | MNFLLSKLLLGLIRFYQYCISPLIPPRCRYTPTCSQYAVEAVKKYGAFKGLRLAIKRIARCHPFGGHGHDPVP | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B4RVQ6 | SYDP_ALTMD | Protein Syd | MALTISAQLDKFVSSYVEHAKGEGLKIAFDSEWPSPCYEETAKDGELVEWAPKRQSPPLSFNNVEDALSLKLHADYCCYFTTYYSDNLKAKAPQGDCELLQVFNREDFERLQQNLIGHLLMKQRLNQAPTLFFGLTDEEDFILTVINETGEVALEQVGQAPTQILANSLAEFIEQLSPLNA | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B4S2L7 | FETP_ALTMD | Probable Fe(2+)-trafficking protein | MARTVFCRKLQKEADGLDFQLYPGELGKRIFDNISKEAWGEWQKKQTMLINEHKLNMMEPNARAFLEEKMSAYLFDDVEPTIEGYVPPEK | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B4S9D2 | HRCA_PROA2 | Heat-inducible transcription repressor HrcA | MKTIDLTPREREVLGIIIQAYVVSASPVSSRFIAKNYNLGLSDATIRNVMADLEDAGFISQPHTSAGRVPTDKGYRYYVDLIMMVQGIDDDEKRHIDSNLRLFTIDRKDSSEVLFAAAKVLGSISQQLSVVMSPRLSLGVFERLDMVLLSSSRIMVILSIQSLFVKTIVMELDLDVSRRQIEMVVDLLNQRLSGLTLDEIRTSIAERLADCDTDQGLLNRIVRSADELFDESPVLDRLYIAGAEYIVSQPEFDQPQKVRDLICMIEDKTRIARIVDLDGVVVPQVMTERDVSITIGRENPASTEGDFTVVTTPYFVGNTM... | 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}. |
B4SS10 | FETP_STRM5 | Probable Fe(2+)-trafficking protein | MSRTVFCQYEQRDAEGLDFVPYPGELGQRIFNNIGKQAWAAWLAHQTMLINENRLSPRTPEHRAFLEGELVKFLFEKDAEKPAGFTPEA | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B4SZX8 | FDHE_SALNS | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEANDQGKPPLDIHVLPRDKHWQKLLHSLIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B4T2U4 | CBPM_SALNS | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B4T381 | NRDI_SALNS | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIRVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLPRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B4T4W0 | SYDP_SALNS | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B4TBW8 | FDHE_SALHS | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEANDQGKPPLDIHVLPRDKHWQKLLHSLIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B4TEN4 | CBPM_SALHS | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B4TEZ3 | NRDI_SALHS | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIQVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLSRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B4TG15 | SYDP_SALHS | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B4TPP6 | FDHE_SALSV | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEANDQGKPPLDIHVLPRDKHWQKLLHSLIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B4TSM2 | CBPM_SALSV | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B4TSY7 | NRDI_SALSV | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIQVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLSRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B4TUI6 | SYDP_SALSV | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B4U1A7 | HRCA_STREM | Heat-inducible transcription repressor HrcA | MITERQSNILNLIVDLFTQTHEPVGSKALQSVIASSSATIRNDMAKLEKLGLLEKAHTSSGRMPSAAGFKYFVEHSLNLGSIDEQDFYQLVKAFDFEAFKLEDVLLRASQMLSDMTGYTAAILDVEPARQRLTGFDIVQLSSHDALAVLTLDESKPLTVQFAIPKNFMNRDLLVLKGIVADRLLGKDVMTVHYKLRTEIPQIVQKYFTVTDNVLDLFDYIFVGLFRETIFVSGKVAALDYAGLVTYQFLDEEQRLALSIRQSLSEEEMATVQVADSSEPALANVTLLTYKFLIPYRGFGLLSLIGPVDMDYRRSVSLINV... | 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}. |
B4U300 | Y1013_STREM | UPF0122 protein Sez_1013 | MKIMEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIAEEFGVSRQAVYDNIKRTEKILEAYEMKLHMYSDYIVRSEIFDDILAKYPSDHYLRDKISILTSIDNRD | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}. |
B4U4M2 | YABA_STREM | Initiation-control protein YabA | MNKKELFDAFDGFSQNLMVTLADIEAMKKQVQGLVEENTILRLENTKLRERLSQLEHENLAKTSSKQGKDHLEGIYDEGFHICNFFYGQRRENDEECMFCRELLDRK | Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}. |
B4U8V6 | YIDD_HYDS0 | Putative membrane protein insertion efficiency factor | MKYLLIKFVRFWQICISPLYPSSCRFYPTCSHYAILSIEKYGAFKGGMKAFWRILRCNPWNKGGIDYP | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B4UJ96 | FETP_ANASK | Probable Fe(2+)-trafficking protein | MARMVMCKKLGRELPGLAYKPFPNELGQRIYDSISQDAWKLWLEHFKMILNEYRLAPADPRTTEILYQQAEQFFFGENAQLPPDYRPPPSKG | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B4UJT7 | HRCA_ANASK | Heat-inducible transcription repressor HrcA | MASADELDRREREILRALVQDYIHTGEPVASQPLLSRHELEWSPATVRSVMADLEALGFLEKPHASSGRIPTERGYRLFVDTMLKVRPPSVADRDRIERLAQAAPDVSSLIEGTADLLHSLSHHAGVVTTPRPQADPVRQLEFVRLRENRVLVVFVSEAGIVTNKLVQLEFAMEPAELERAAAYLNEKLHARADAAELAALRAAILTDMRADQSALHDLLQKALVLAEQSFAGTGVEKVVMEGESSFLDAPEFSDVQKARALLRGFAEKDRILRVLDRVLTAQEVQIFIGAESEFATVPDVSVVAAPYGRGDRVLGTLAV... | 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}. |
B4UKG2 | YIDD_ANASK | Putative membrane protein insertion efficiency factor | MIRAALVLLVRIYQRLVSPLLPPACRFYPSCSAYAVTALQRHGALRGSWLTVRRLCRCHPFHAGGVDPVPELTPKR | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B4UN34 | SPG4_CANGA | Stationary phase protein 4 | MPSFWDSFAVYNRNKHAKGDVHGGHMSQNMGGQPMYLQAKEHADIKKKEDGTLEAKIETPDGPRLVDVSNMTQQEFERTYNSLRKGEPNNRVNF | Stationary phase-essential protein not required for growth on nonfermentable carbon sources. |
B5BBH3 | CBPM_SALPK | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNTDWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B5BEM1 | NRDI_SALPK | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIRVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKYGVPWLYRFELMGTQRDIDNVRRGVNEFWQQLPRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5BF22 | SYDP_SALPK | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5BG08 | GLGS_SALPK | Surface composition regulator | MNNNNVYSLNNFDFLARSFARMQAEGRPVDIQAVTGNMDEEHRDWFCKRYALYCQQATQAKKLELEH | Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}. |
B5BIL7 | YIDD_SALPK | Putative membrane protein insertion efficiency factor | MAPPLSPGSRVLIALIRVYQRLISPLLGPHCRFTPTCSSYGIEALRRFGVIKGSWLTVKRVLKCHPLHPGGDDPVPPGPFDTREH | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B5BJF4 | FDHE_SALPK | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEANDQGKPPLDIHVLPRDKHWQKLLHSLIAELKPEMNGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIDTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5E0H4 | SMG8_DROPS | Nonsense-mediated mRNA decay factor SMG8 (Protein smg-8 homolog) | MGLKDYYTWKFPNIPEHVAQELDQLGRSLVVVGVIGRSRCVLANKMRAFGMEPPVDHEPTDGQLQCYYKPGTSTLLLHFETTFDDAILGQQIDETMEQDGAPFDFDGFYERMKCRFVRMMLLALHVCHILVYVETGQTFDLSLVTIFQLMKFGREHHLIQFLPSLLKETPAGRLLGEKCRLCTPRILFLFENFTQEEGKTRECVSACEFQTEDSIYELLRHHQIITNSSSSSLLALPNNKQFVFYNAHDQLHADRLLQSIEFLNLDMRKVDVKEEDDDLEVLELAPFNGFVKSFGESFENTNYEEQQYKTEHTAWHFLQR... | Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity). |
B5E1Y5 | YIDD_STRP4 | Putative membrane protein insertion efficiency factor | MKRILIAPVRFYQRFISPVFPPSCRFELTCSNYMIQAIEKHGFKGVLMGLARILRCHPWSKTGKDPVPDHFSLKRNQEGE | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B5E230 | HRCA_STRP4 | Heat-inducible transcription repressor HrcA | MVTERQQDILNLIIDIFTKTHEPVGSKALQESINSSSATIRNDMAELEKQGLLEKAHTSSGRMPSVAGFQYYVKHSLDFDRLAENEVYEIVKAFDQEFFKLEDILQEAANLLTDLSGCTVVALDVEPSRQRLTAFDIVVLGQHTALAVFTLDESRTVTSQFLIPRNFLQEDLLKLKSIIQERFLGHTVLDIHYKIRTEIPQIIQRYFTTTDNVIDLFEHIFKEMFNENIVMAGKVHLLNFANLAAYQFFDQPQKVALEIREGLREDQMQNVRVADGQESCLADLAVISSKFLIPYRGVGILAIIGPVNLDYQQLINQVNV... | 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}. |
B5E439 | YABA_STRP4 | Initiation-control protein YabA | MDKKELFDALDDFSQQLLVTLADVEAIKKNLKSLVEENTALRLENSKLRERLGEVEADAPVKAKHVRESVRRIYRDGFHVCNDFYGQRREQDEECMFCDELLYRE | Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}. |
B5E525 | Y1182_STRP4 | UPF0122 protein SPG_1182 | MEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIAEEFGVSRQAVYDNIKRTEKILEDYEMKLHMYSDYIVRSQIFDQILERYPKDDFLQEQIEILTSIDXRE | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}. |
B5EPX1 | FETP_ACIF5 | Probable Fe(2+)-trafficking protein | MSRMVQCVKLGHEAEGLDRPPYPGALGARIYQEVSKEAWQGWLKHQTMLINEYRLSPIDPKSRTFLEKQMEAYFFGDGAQSPEGYVPPAPQDS | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B5F008 | FDHE_SALA4 | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEANDQGKPPLDIHVLPRDKHWQKLLHSLIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5F1Z4 | CBPM_SALA4 | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B5F333 | NRDI_SALA4 | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIQVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLPRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5F4R1 | SYDP_SALA4 | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5F9R3 | FETP_ALIFM | Probable Fe(2+)-trafficking protein | MSRTVFCVRLNKEADGLDFQLYPGELGKRIFDNISKEAWGQWQHKQTMLINEKKLNMMDPEHRKLLETEMEGFLFDGKDVVIDGYTPPSE | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B5FAU2 | SYDP_ALIFM | Protein Syd | MPLSVEQALANFSQRYVEAWKAQHDCLPINEELVGLASPCIEETRDLEISWQPIVRDEAIRLHNIEQGIELDLHDDFHAFYGTQYSADMTAKFEDMNIELLQVWSDEDLERLQGNMLGHLVMQRRLKLVPTLFVAVTDDEMEVVSICNQSGEVILERVGTKNRTVLAANMAEFLNKLEPVIAA | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5FP25 | FDHE_SALDC | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLRMDLTARIKDANDQGKPPLDIHVLPRDKHWHTLLHSMIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPLIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5FR39 | CBPM_SALDC | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B5FSW2 | NRDI_SALDC | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIRVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLSRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5QUL6 | NRDI_SALEP | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIQVDEPYILVVPSYGGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLSRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5QUQ3 | YIDD_SALEP | Putative membrane protein insertion efficiency factor | MAPPLSPGSRVLIALIRVYQRLISPLLGPHCRFTPTCSSYGIEALRRFGVIKGSWLTVKRVLKCHPLHPGGDDPVPPGPFDTREH | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B5QWQ1 | SYDP_SALEP | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5QWW9 | FDHE_SALEP | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLRMDLTARIKDANDQGKPPLDIHVLPRDKHWHTLLHSMIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5QZ33 | GLGS_SALEP | Surface composition regulator | MNNNNVYSLNNFDFLARSFARMQAEGRPVDIQAVTGNMDEEHRDWFCKRYALYCQQATQAKRLELEH | Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}. |
B5R048 | CBPM_SALEP | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B5R6G2 | CBPM_SALG2 | Chaperone modulatory protein CbpM | MANITVTFTITEFCLHTGVTEEELNEIVGLGVIEPYEDDNADWQFDDRAASVVQRALRLREELALDWPGIAVALTLLEENSRLREENRLLLQRLSRFISHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B5RDD6 | NRDI_SALG2 | Protein NrdI | MSALVYFSSSSENTHRFMQRLGLPATRIPLNERERIQVDEPYILVVPSYGGGMAGAVPRQVIRFLNDEHNRARIRGVIASGNRNFGDAWGCAGDVIAQKCGVPWLYRFELMGTQRDIDNVRKGVNEFWQQLSRSA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5RDU5 | SYDP_SALG2 | Protein Syd | MDELTAQALKAFTTRYCDAWQEKHGSWPLSEELYGVPSPCIISSTRDAVYWQPQPFEGEENVNAVERAFDIMVQPALHAFYTTQFAGDMPAQFADEKLTLLQTWSQDDFRRVQENLIGHLVTQKRLKLPPTLFIATQENELEVISVCNLSGEVIKETLGTRNRTVLAATLAEFLTQLNPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5RFD8 | FDHE_SALG2 | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNVYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLRMDLTARIKDANDQGKPPLDIHVLPRDKHWHTLLHSMIAELKPEMSGPALAVIENLEKASEQELEQMASALFASDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEARQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLENEQAAVKAESCGDCGTYLKILYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5RFY4 | YIDD_SALG2 | Putative membrane protein insertion efficiency factor | MAPPLSPGSRVLIALIRVYQRLISPLLGPHCRFTPTCSSYGIEALRRFGVIKGSWLTVKRVLKCHPLHPGGDDPVPPGPFDTREH | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B5RMX7 | SP5G_BORDL | Putative septation protein SpoVG | MNITNVRIRRVDNKDSSSKLLAYVTVTFDDCLVLHNIRVIRGQKGVFIVMPNRRTKIGEYKDIVHPINQSFREILQSAIFKEYVKENPSNFELELV | Could be involved in septation. {ECO:0000255|HAMAP-Rule:MF_00819}. |
B5RQC2 | SP5G_BORRA | Putative septation protein SpoVG | MNITNVRIRRVDNKDSSSKLLAYVTVTFDDCLVLHNIRVIRGQKGVFIVMPNRRTKVGEYKDIVHPINQSFREILQSAIFKEYVKENPANFELELV | Could be involved in septation. {ECO:0000255|HAMAP-Rule:MF_00819}. |
B5VFW2 | RRG1_YEAS6 | Required for respiratory growth protein 1, mitochondrial | MAQNFGKIPSHKSYVLSLYRTVLRNIPKCCHSYAFQYEIKKTLSKQLFKHKHDKSSWSVYTLLNEFSLLNNCLLEGKLQEIKNLMKPLKKMKKQLETTKILNSLTSLGDVKTNDPEEVRRFHVLSAYIKRKQDLGLLPAYIPKTYQHKLLLPLALNEHACLKLFHIQQKLKNGPPSAGLSYTKEGRNQIWFVRSPINKGRQQSKKLGILIRKERKDSQKNIDNLNFCEINAAWALHEAIWEEYLESKKIIKVNLPKYLEYAANIPKSTKCNPSSQYQKIKEWVDPVREIMFELHSKSFQRVEYFNKYKEKLLKNGGQLAY... | Essential for respiratory growth and required for mitochondrial protein synthesis. Required for vacuolar acidification (By similarity). |
B5VI68 | IRC6_YEAS6 | Increased recombination centers protein 6 | MVLQYPQNKILVLSDHPHNFSKTQFLQDLFHCSSTGISIVKDQTWENRYYKVHFDLYIDSCKDIPVWVEEFITPECEPLRNVMAGIILITDIRQTKPQELLHQFMIAAHRNTFVVLVNVNEEVEQDEIDELNEIWSNAFTNVIELVNWKRSKPTVNHNDYGEKLGLDRIQEIIDTHDWLNCEVLPATKIREEIPNEMPLEQIIRNLQSARLKYKSIENSSEADAFANEMADELSRYL | Involved in gross chromosomal rearrangements (GCRs) and telomere healing. |
B5VM60 | MTC2_YEAS6 | Maintenance of telomere capping protein 2 | MGDHNLPDFQTCLKFSVTAKKSFLCMYRDSVSKEKLASSMPSTCDIQLKRAINDAYPGGGIKVTVLNSTTASLDSLATTHVKEFEIVIIPDINSLLQPDQAKLVKIMRDCTVAIEKAQSTRIFIGVVHWNNPVQPSGAAKDGDEAGKPAPKTRIFLPTSLRMGAWLKHKFWFACAPPYLDFESSTESSINTRANNSIGMAEEEKQEPESKRSIILNEEANLNDVFVGSTVRRYILDIMVHLRTHRLTYNAKAGGVYTNSLDDVVLLSRLIGLHSGKMFVSPSHVKEASRWYFPMHLELVQRSSMDSSLLYGSDPNLVDEM... | May be involved in telomere capping. |
B5VMR4 | IRC19_YEAS6 | Increased recombination centers protein 19 | MRKPSITITTAKAIITPDYTLIKSHSKYQLPSRFQKLDADSPERSTVVKLFYRRFMRLKPFISNVKMVKDTYRDYVRYKFMKENYELKRYLVFNPDGLRSKIKVELLSNTKCCEKILPVTEMQRTLEFVLKSCSYLPETKAQKWDIARDNTYCRQILKNLLTMQYEKYRSILHRGIGHDELDVKFSHLKTTSSPLTKLNKTEKKKIPLFKVFSDFDTTLIYLNETLGTRL | Involved in sporulation and maintenance of the mitochondrial DNA. Is probably involved in a pathway contributing to genomic integrity (By similarity). |
B5VTQ6 | RRG8_YEAS6 | Required for respiratory growth protein 8, mitochondrial | MGLPKSAYKKLLIDCPTRVINKNCAQRVKDVSPLITNFEKWSDKRKKLYFKDEEEMVGHFHLENFNLKNNLYGRLLASPMRAEKISKLKSCRELLIPLKVVPSTGKDQHADKDKLKLVPTLDYSKSYKSSYVLNSASIVQDNLAAATSWFPISVLQTSTPKSLEVDSSTFITEYNANLHAFIKARLSVIPNVGPSSINRVLLICDKRKTPPIEIQVVSHGKGLPITQSVFNLGYLHEPTLEAIVSKDAVTKGIYLDADNDKDLIKHLYSTLLFQSVN | Required for respiratory activity and maintenance and expression of the mitochondrial genome. |
B5XJY1 | YIDD_STRPZ | Putative membrane protein insertion efficiency factor | MKKLLIVSVKAYQKYISPLSPPSCRYKPTCSAYMLTAIEKHGTKGILMGIARILRCHPFVAGGVDPVPEDFSLMRNKNTSKNAEKA | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B5XK03 | YABA_STRPZ | Initiation-control protein YabA | MNKKELFDAFDGFSQNLMVTLAEIEAMKKQVQSLVEENTILRLENTKLRERLSHLEHETVAKNPSKQRKDHLEGIYDEGFHICNFFYGQRRENDEECMFCRELLDRK | Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}. |
B5XK14 | NRDI_STRPZ | Protein NrdI | MAELIIVYFSSKSNNTHRFVQKLGLPAQRIPVDNRPLEVSTHYLLIVPTYAAGGSDAKGAVPKQVIRFLNNPNNRKHCKGVISSGNTNFGDTFALAGPIISQKLQVPLLHQFELLGTATDVKKVQAIFARLKHHTHDKQKQTNNLITERTHPCHKPMRHTSH | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5XLN6 | Y946_STRPZ | UPF0122 protein Spy49_0946c | MNIMEIEKTNRMNALFEFYAALLTDKQMNYIELYYADDYSLAEIADEFGVSRQAVYDNIKRTEKILETYEMKLHMYSDYVVRSEIFDDMIAHYPHDEYLQEKISILTSIDNRE | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}. |
B5XU89 | FETP_KLEP3 | Probable Fe(2+)-trafficking protein | MSRTIFCTFLQREADGQDFQLYPGELGKRIYNEISKEAWAQWQHKQTMLINEKKLSMMSPEHRKLLEQEMVQFLFEGKDVHIEGYTPPEKQ | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}. |
B5XV06 | SYDP_KLEP3 | Protein Syd | MDHQTAEALRAFTQRYCAAWQQQRNSLPRSEELYGVPSPCVVDTQGEAVFWQPQPFSLAQNISAVERALDIVVQQPLHSYYTTQFAGDMTGRFADETLTLLQTWSEEDFQRVQENLIGHLVVQKRLKLAPTLFIATLESGRDVISVCNLSGEVIKETLGTAKRITLSPSLASFLSHLEPVL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5XVD7 | NRDI_KLEP3 | Protein NrdI | MSLIVYFSSRSENTHRFVQRLGLPAVRIPLNEREHLQVDEPYILIVPSYGGGGTAGAVPRQAICFLNDVHNRQLIRGVIAAGNRNFGDAWGRAGEVIAQKCAVPYLYRFELMGTPDDIDNVRKGVSEFWQRQPQNV | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5XZH9 | FDHE_KLEP3 | Protein FdhE homolog | MSIRIIPQDELGSSEKRTAEAIPPLLFPRLKNLYNRRAERLRELAANNPLGDYLRFAALIAHAQEVVLYDHPLQMDLTARIKAASEQGKPPLDIHVLPRDKHWHKLLHSLIAELKPEMSGPALAVIENLEKASEQELEQMASALFVSDFASVSSDKAPFIWAALSLYWAQMASLIPGKARAEYGEQRQFCPVCGSMPVSSIVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSRDLHYWSLDNEQAAVKAESCGDCGTYLKIMYQEKDPKVEAVADDLASLVLDARMEQEGFARSSINPFMFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5YBN7 | YIDD_DICT6 | Putative membrane protein insertion efficiency factor | MRGLLIILIKFYKKFISPVLPKSCRFYPTCSTYALEAIERFGAFEGGILAIKRILRCHPFNPGGYDPVPTKEEFLELKLKRRKNK | Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. |
B5YR89 | GLGS_ECO5E | Surface composition regulator | MDHSLNSLNNFDFLARSFARMHAEGRPVDILAVTGNMDEEHRTWFCARYAWYCQQMMQTRELELEH | Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}. |
B5YU42 | CBPM_ECO5E | Chaperone modulatory protein CbpM | MANVTVTFTITEFCLHTGISEEELNEIVGLGVVEPREIQETTWVFDDHAAIVVQRAVRLRHELALDWPGIAVALTLMDDIAHLKQENRLLRQRLSRFVAHP | Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ. {ECO:0000255|HAMAP-Rule:MF_01155}. |
B5YZ28 | FDHE_ECO5E | Protein FdhE | MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE | Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}. |
B5Z288 | NRDI_ECO5E | Protein NrdI | MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA | Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}. |
B5Z3F8 | SYDP_ECO5E | Protein Syd | MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLAPNLAEFLNQLKPLL | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}. |
B5ZAX5 | Y158_UREU1 | UPF0122 protein UUR10_0158 | MLNKNKRWYLIALYDIYQGLLTTKQCEYFNLHYFKDLSFSEIAELKEVSKSAISDCLNKVCDQLLKYEQALLIYEKNKKRNDLYTLINDSELVKKLKDI | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}. |
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