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
|
MLTKRQLLVLKEIIRLFTESGQPVGSKTLMQELPVHVSSATIRNDMAALEDAGLITKTHSSSGRVPSTQGYRYYLDHLVEPVRVSRHDLATIKQELGQRYSKMDEIVAQSVQILSNLTSYTAISLGPEVNNIKLTGFRLVPLGNHQVMAILVTNNGNVENQVFTVPPSISSDELEKAIRIVNDQLVGLPLVQVAQRLRTDVPSMLMQYLTSPDGFLDIFGNVLKSAASERFYVGGRLNLMDYLGDSDIHELKKIMSLIDADHGDLTELLGGPIRQTPVQVRLGPELKPIDLANLSLITASYDVGGHGTGMIALLGPTQMPYSKMIGLLDVFREELAKRLTDYYANFDQ
|
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)
|
MGLKDYYTWTFPNIPEHVAQELDQLGRSLVVVGVIGRSRCVLANKMRAFGMEPPVDHEPTDGQLQCYYKPGSSTLLLHFETTFDDAILGQQIDETMEQDGAPFDFDGFYERMKCRFVRMMLLALHVCHILVYVETGQTFDLSLVTIFQLMKFAREQHLMQFLPSLLKETPAGRLLGEKCRLCTPRILFLFENFTHEEGKTRECVSACEFQTEDSIYELLRHHQIITNSSSSSLLALPNNKQFVFYNAHDQLHADRLLQSIEFLNLDMRKLDVKEEEDDLEVLELAPFDGFVKSFGESFESTNYEEQQYKTEHTAWHFLQRHVQDALLGCFDEGSFKQVPQRGQLQLLNAQEWHDCIAELHKLLVSSAGTQESLNEIRNEDYQVFLQSFDESLNYEKKFWAHLCEIGLKMGIEAYKKAAPAIYGSSMHQQLLAEATLAFEEEGRGPPAEASIAKMTATCLRHWQDGRQQCEQLSLRSQPCTQPKEMPHDKHNSGVIHVSSCNCGRTQGRREDPFSLRQANYEFYEHMVKMCNLCVKVKQFKFPIFEPTNNEYRAAAFEVAFPLLHAGKNRLAQDAELDPDEEDEELPTGEREEQHITQSNGCSQPLSPTFGSDLNMSIAGFGVSLNESEPCFDQSSSSEAESTCSGTSSEESNNELVLQLKEPAKKHEESCDPDSIAPLPSMCLTSTTEYLPGLVHTLSKVGLLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVQLRLVHASKHYHNSHQPHMSKKQQRYRKHGDRMVLKIFVGFEYECSRGHRFMMCRPDRVLRGGADIERDTCSKMVHTNMPLYYPCPCRSQNNYLAQLMRIHVVTPKAPVNIIVDPKVCMGKDKYTFTLGSMVPPRLSQSAYWILRLPYVYQGDDALIAPPEKLEPDDIMAGGYLLAGMFGIAETDPTLDLNDQGHLDTNELGTFTRI
|
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
|
MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRIMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCTLNSSGGMDAQWTQGGTEVACIKGGAAIKECAVLNDKRYIITKDSQDQVVVYDVLRVVKKEQLGAVDYEAEVKKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFSAWVSIEAGLPECVDPTTEIKINYGKLLLEALLEYWTPPHSIPPNEMEPDMHGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIEKNIPKFLKIPFFLQPHPQMTKPERTKKDRLVANEFIQCRKVCEHVLEKVLNAETTPSGGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVVVDPNMDLRTVRHFIWKQSTDLTFQYKTKQNFNYDGSIGDSLERVTRKY
|
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)
|
MLDDYYTWTYPDIPENVAQELLQLNGSLVVVGVVGRSDCDLANKMLAFGMEPPDDHTPEDGQIQCYYKPGTFSLLLHFESTYDAEISGQMIDVCIEDVDTPFDIDSFFERIRCRFVRMMLLALHVCHIVVWAKFAREQHLMQFLPQMLRETPAARISERTRLCAPRILFLFENFPGDEPKTRESVSTCEFQMEDCIYELLRRYNIVTNSSSNSLVALPNNKQFVFFNAHEELRDDKLLKAIDCLNETMYKPDLKEEEEDLEILAMAPFDGFVKPFTMPVYEKEWENLQYQEDHTVWNFLQRHVHDALVGCFDAGSFKQHAQQGPFQLLNSREWHDCMATMHKLLVENAKDPDHETSNEEYKLFLKNFDEDLNYEKKFWAHLCELGLKKGIAAYKNAAPANYGTATHRQLLADATLAFEEEGRGPQAQAALAKLAAICHKHWEDGRQQCEQLSLRSHPCTLPKNMPHEKHNSGVIHISTCNCGRTQGRREDPFNLRQANYEFYEHIAQMCNLCVKVKQYQFPIFEPSVSDYRAAAFEAAFPLLNTGKSGAPQDEDAGEDEAEEEEGQERELPTKKQLQNTASNCCSHPLSPTFGSDLNMSIAGFGASLKESQARSEQLSNSEQNTTRSGSSSVDTENELVVELQEPAKKEAREDVGPTDAVSTSTTEYLPGLVHTVSNFDLLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVQLRLVHALKQQYQHHHHGKKQQRWKKQGDRLSLKIFVGMEYECSRGHRFMMCAPDRVLRGGADIERDTCSKVVHNNMPLYYPCPCRSQKNFLAQLMRIHVVTPKAPVNIIVDPKVCVGRYTFTLGSILPPRLSQSAYWIIRLPYVYQGDDVLIAPPDQLDPDYPLAGGYLLPGMFGVVETDPTLDLNEPGMMGASAAGNFTRI
|
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
|
MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDPNNGKLYSAGRDAIIRVWNTRTESNEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAHKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCIQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEIRNPSNKMLVCEEKAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCILTSGGMDAQWTLGGTEMACIRGGAAIKECTVLNDKRYIITKDSQDKVVVYDVLRVIKKEELGPIEYEKEVMKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFSAWVSIEAGLPECDDPTTEIKINYGKLLLEALLEYWTPPHSIPPNEMEPDVRGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIERNIPKFLKIPFFLQPHPQMTKPERSKKDRLVANEFIQCRKVCEHVLEKVLNTETTPSGGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVVVDPNMDLRTVRHFIWKQSTDLTFQYKAKQNFNFDGK
|
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
|
MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDSNNGKLYSAGRDAIIRVWNTRTEANEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAHKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCIQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKMLVCEEKAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCVLSSGGMDAQWTLGGTELACIKGGAAIKECTVLNDKRYIITKDSQDQVVVYDVLRVTKKEELGVVDYEEEVKKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFAAWVSIEAGLPECDDPTTEIKINYGKLLLEALLEYWTPPHSMPPNEMEPDVRGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIERNIPKFLKIPFFLQPHPQMTKPERTKKDRLVANEFIQCRKVCEHVLEKVLNAETTPSAGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVIVDPNMDLRTVRHFIWKQSTDLTFQYKTKQNFNFDGSIGDSLERVTRKY
|
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)
|
MSYKNYYTWKYPDIPEHVAPLLLELQNSLVIVGIIGRSKCAQANKMSAFGMQPDKTHEPADGQILCYYKPGTNMLLLHFETTHDEAVLGQQLLKQTSVDFDSFYEQMRSRFLRMLLLALHVCHILVYVETAQTFDTTLVTICQLLKYVREKHVLDFLPQMLRETAAGSLLSDRARLCTPRVLFLFENYPQDEEKSRERISAYEFQTEDKIYELLRQYNIVTNNANNSLFALPNNKQFVFYNAHEKLRPDQLLLAIEALNATMYKSDSKEEEEDTEILELAPFEGFVKPYGAGYEARESDEQLYRKKHTVWHFLQRHVQDALQGCFDEGSFKQLPQSAQFQLLGVNDWHICMDTIHRLLIGNIQEVSYVTNNQNYKAYLRDFNESLNYEKKFWGHLCDLGLKKGISAYKSSAPAIYGSVTHRQLLADAILAFEEEGRGPYAELALAKLSEICLRHWHDGRQQCEQLSLRGNPCTQPKDAPHDKHSSGIVHISSCNCGRTQGRREDPFTLRQANYDYYEHMAAMCNLCVKVKKFQLPVFTPSISDYRAAAFEAAFPLLLQAAKNRTEIATGGDSDLEAAGELYSQPINATEQAPQKPQITLSNGCSQPALSATYGSDLNMSIAGFGASLNEGEEVRSPEISSQIASSGLSSRSNSTSSGTSSANTANELVLQLKERTDQNAANAAVSEICPEALPIVASTEQVSTTEYLPGLVHMSSGCELLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVHVRLVQPHKHPQQQQQSMGKKSQRYRKHGDRLALKIFVGFEYECSRGHRFMMCSPDRVLRGGADIERDTSSKVVNNNMPLYFPCPCRAQPTYLAQLMRIHVVTPKAPVNIILDPKMCVGKYTFTLGCPTLPRLSQSAYWILRLPYVYQGDNVLITPPERLEPDDNMASGCLLAGMFGIAETDTNETNQQAITPLTFTRL
|
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
|
MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDSNNGKLYSAGRDAIIRVWNTRTESNDKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAHKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCIQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKMLVCEEKAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCTLSSGGMDAQWTMGGTELACIKGGAAIKECTVLNDKRYIITKDSQDQVVVYDVLRVIKKEELGPVDYEEEVKKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFAAWVSIEAGLPECDDPTTEIKINYGKLLLEALLEYWTPPHSMPPNEMEPDVRGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIERNIPKFLKIPFFLQPHPQMTKPERTKKDRLVANEFIQCRKVCEHVLEKVLNAETTPSGGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVIVDPNMDLRTVRHFIWKQSTDLTFQYKTKQNFNFDGK
|
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
|
MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRSMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIVSGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCTMNSSGGMDAQWTQGGTEVACIKGGAAIKECAVLNDKRYIITKDSQDQVVVYDVLRVVKKEQLGAVDYEAEVKKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFSAWVSIEAGLPECVDPTTEIKINYGKLLLEALLEYWTPPHSIPPNEMEPDMHGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIEKNIPKFLKIPFFLQPHPQMTKPERTKKDRLVANEFIQCRKVCEHVLEKVLNAETTPSGGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVVVDPNMDLRTVRHFIWKQSTDLTFQYKTKQNFNYDGSIGDSLERVTRKY
|
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)
|
MLDDYYTWTYPDIPENVAQELLQLNGSLVVVGVVGRSDCDLANKMLAFGMEPPDDHTPEDGQIQCYYKPGTFSLLLHFESTYDAEISGQMIDVCIEDVDTPFDIDSFFERIRCRFVRMMLLALHVCHIVVYVENGLTFDPTLLTVFQLAKFAREQHLMQFLPQMLRETPAARISERTRLCAPRILFLFENFPGDEPKTRESVSTCEFQMEDCIYELLGRYNIVTNSSSNSLVALPNNKQFVFFNAHEELRDDKLLKAIDCLNETMYKPDLKEEEEDLEILAMAPFDGFVKPFTMPVYEKEWENLQYQEDHTVWNFLQRHVQDALVGCFDAGSFKQHAQQGPFQLLNSQEWHDCMATMHKLLVENAKDPDHETSNEEYKLFLKNFDEDLNYEKKFWAHLCELGLKKGIAAYKNAAPANYGTATHRQLLADATLAFEEEGRGPQAQAALAKLAAICHNHWEDGRQQCELLSLRSHPCTLPKNMPHEKHNSGVIHISTCNCGRTQGRREDPFNLRQANYEFYELIAQMCNLCVKVKQYQFPIFEPSVSDYRAAAFEAAFPLLNTGKSGAPQDEDAGEDEAEEEEGQERELPTKKKLQNTASNCCSHPLSPTFGSDLNMSIAGFGASLKESQASSEQLSNSEQNTTSSGTSSADTENELVVELQEPAKKEAREDVGPTDAVSTSTTEYLPGLVHTVSNFGLLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVQLRLVHALKQQYQQQHHGKKQQRWKKQGDRLSLKIFVGMEYECSRGHRFMMCAPDRVLRGGADIERDTCSKVVHNNMPLYYPCPCRSQRNFLAQLMRIHVVTPKAPVNIIVDPKVCVGRYTFTLGSIVPPRLSQSAYWIIRLPYVYQGDDVLIAPPDHLDPDYPLAGGYLLPGMFGVVETDPTLDLNEPGMMGASAAGNFTRI
|
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
|
MLTHKTCQARKKMQVSFVIRDAEEKQHRNGVNALQLDANNGKLYSAGRDAIIRVWNTRTDSSEKYIQSMEHHNDWVNDIVLCCNGRNLISASCDTTVKVWNAQKGFCMSTLRTHRDYVQALAYAKDREQVASAGLDKAIFLWDVNTLTALTASNNTVTTSSLTGSKDSIYSLAMNPSGTVIVSGSTENILRIWDPRTCMRIMKLRGHTENVRCLVVSPDGNQVVSGSSDGTIKVWNLGQQRCVQTIHVHKEGVWSLLMSENFQYIISGSRDRNIIVTEMRNPSNKTLVCEEQAPVLSLGYNIDKTGVWATTWNSDIRCWKLPMYDRCTLNSSGGMDAQWTQGGTEVACIKGGAAIKECAVLNDKRYIITKDSQDQVVVYDVLRVVKKEQLGAVDYEAEVKKRNKQVYIPNWFTVDLKTGMPTIVLGQEEVDCFSAWVSIEAGLPECVDPTTEIKINYGKLLLEALLEYWTPPHSIPPNEMEPDMHGNGYFQVPKHTPVIFSEVGGRTVCRLLVRDAAGDSESTLLHETAPQWVTDVVIEKNIPKFLKIPFFLQPHPQMTKPERTKKDRLVANEFIQCRKVCEHVLEKVLNAETTPSGGNANNSLQNSQSDANSEGSQLPAEERIELWCNDVVVDPNMDLRTVRHFIWKQSTDLTFQYKTKQNFNYDGK
|
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
|
MKTIDLTPREREVLGIIIQAYVVSASPVSSRFIAKNYNLGLSDATIRNVMADLEDAGFISQPHTSAGRVPTDKGYRYYVDLIMMVQGIDDDEKRHIDSNLRLFTIDRKDSSEVLFAAAKVLGSISQQLSVVMSPRLSLGVFERLDMVLLSSSRIMVILSIQSLFVKTIVMELDLDVSRRQIEMVVDLLNQRLSGLTLDEIRTSIAERLADCDTDQGLLNRIVRSADELFDESPVLDRLYIAGAEYIVSQPEFDQPQKVRDLICMIEDKTRIARIVDLDGVVVPQVMTERDVSITIGRENPASTEGDFTVVTTPYFVGNTMGRLAVLGPKRMDYARVVRVVNYMADRLSTTFSDVN
|
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
|
MITERQSNILNLIVDLFTQTHEPVGSKALQSVIASSSATIRNDMAKLEKLGLLEKAHTSSGRMPSAAGFKYFVEHSLNLGSIDEQDFYQLVKAFDFEAFKLEDVLLRASQMLSDMTGYTAAILDVEPARQRLTGFDIVQLSSHDALAVLTLDESKPLTVQFAIPKNFMNRDLLVLKGIVADRLLGKDVMTVHYKLRTEIPQIVQKYFTVTDNVLDLFDYIFVGLFRETIFVSGKVAALDYAGLVTYQFLDEEQRLALSIRQSLSEEEMATVQVADSSEPALANVTLLTYKFLIPYRGFGLLSLIGPVDMDYRRSVSLINVIGQLLAVKLRDYYRYLNSNHYEVH
|
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
|
MASADELDRREREILRALVQDYIHTGEPVASQPLLSRHELEWSPATVRSVMADLEALGFLEKPHASSGRIPTERGYRLFVDTMLKVRPPSVADRDRIERLAQAAPDVSSLIEGTADLLHSLSHHAGVVTTPRPQADPVRQLEFVRLRENRVLVVFVSEAGIVTNKLVQLEFAMEPAELERAAAYLNEKLHARADAAELAALRAAILTDMRADQSALHDLLQKALVLAEQSFAGTGVEKVVMEGESSFLDAPEFSDVQKARALLRGFAEKDRILRVLDRVLTAQEVQIFIGAESEFATVPDVSVVAAPYGRGDRVLGTLAVVGPTRMNYARVIPLVDLTARQISRALAALSEGG
|
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)
|
MGLKDYYTWKFPNIPEHVAQELDQLGRSLVVVGVIGRSRCVLANKMRAFGMEPPVDHEPTDGQLQCYYKPGTSTLLLHFETTFDDAILGQQIDETMEQDGAPFDFDGFYERMKCRFVRMMLLALHVCHILVYVETGQTFDLSLVTIFQLMKFGREHHLIQFLPSLLKETPAGRLLGEKCRLCTPRILFLFENFTQEEGKTRECVSACEFQTEDSIYELLRHHQIITNSSSSSLLALPNNKQFVFYNAHDQLHADRLLQSIEFLNLDMRKVDVKEEDDDLEVLELAPFNGFVKSFGESFENTNYEEQQYKTEHTAWHFLQRHVQDALLGCFDEGSFKQVPQRGQLQLLNAQEWHDCIAELHKLLVSSAGTQESLNEIRNEDYQVFLQSFDESLNYEKKFWAHLCEIGLKMGIEAYKKAAPAIYGSSMHQQLLAEATLAFEEEGRGPPAEASIAKMTATCLRHWQDGRQQCEQLSLRSQPCTQPKEMPHDKHNSGVIHVSSCNCGRTQGRREDPFSLRQANYEFYEHMVKMCNLCVKVKQFKFPIFEPTNNEYRAAAFEVAFPLLHAGKNRLAEDAELDPDEEDEELPTGEREEQHITQSNGCSQPLSPTFGSDLNMSIAGFGVSLNESEPCFDQSSSSEAESTCSGTSSEESNTELVLQLKEPAKKHEESCDPDSIAPLPSMCLTSTTEYLPGLVHTLSKVGLLPLFPSWSLACVGPSSIYSHNTGLQEHFQSGFLSGANFLLPWDVQLRLVHATKHYHNSHQPHMSKKQQRYRKHGDRMVLKIFVGFEYECSRGHRFMMCRPDRVLRGGADIERDTCSKMVHTNMPLYYPCPCRSQNNYLAQLMRIHVVTPKAPVNIIVDPKVCMGKDKYTFTLGSMVPPRLSQSAYWILRLPYVYQGDDALIAPPEKLEPDDIMAGGYLLAGMFGIAETDPTLDLNDQGHLDTNELGTFTRI
|
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
|
MVTERQQDILNLIIDIFTKTHEPVGSKALQESINSSSATIRNDMAELEKQGLLEKAHTSSGRMPSVAGFQYYVKHSLDFDRLAENEVYEIVKAFDQEFFKLEDILQEAANLLTDLSGCTVVALDVEPSRQRLTAFDIVVLGQHTALAVFTLDESRTVTSQFLIPRNFLQEDLLKLKSIIQERFLGHTVLDIHYKIRTEIPQIIQRYFTTTDNVIDLFEHIFKEMFNENIVMAGKVHLLNFANLAAYQFFDQPQKVALEIREGLREDQMQNVRVADGQESCLADLAVISSKFLIPYRGVGILAIIGPVNLDYQQLINQVNVVNRVLTMKLTDFYRYLSSNHYEVH
|
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
|
MAQNFGKIPSHKSYVLSLYRTVLRNIPKCCHSYAFQYEIKKTLSKQLFKHKHDKSSWSVYTLLNEFSLLNNCLLEGKLQEIKNLMKPLKKMKKQLETTKILNSLTSLGDVKTNDPEEVRRFHVLSAYIKRKQDLGLLPAYIPKTYQHKLLLPLALNEHACLKLFHIQQKLKNGPPSAGLSYTKEGRNQIWFVRSPINKGRQQSKKLGILIRKERKDSQKNIDNLNFCEINAAWALHEAIWEEYLESKKIIKVNLPKYLEYAANIPKSTKCNPSSQYQKIKEWVDPVREIMFELHSKSFQRVEYFNKYKEKLLKNGGQLAYFDKKSKEMYAKRLTLFRKMSKETLPYVTLFIEGRDLPSVLAKYGF
|
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
|
MGDHNLPDFQTCLKFSVTAKKSFLCMYRDSVSKEKLASSMPSTCDIQLKRAINDAYPGGGIKVTVLNSTTASLDSLATTHVKEFEIVIIPDINSLLQPDQAKLVKIMRDCTVAIEKAQSTRIFIGVVHWNNPVQPSGAAKDGDEAGKPAPKTRIFLPTSLRMGAWLKHKFWFACAPPYLDFESSTESSINTRANNSIGMAEEEKQEPESKRSIILNEEANLNDVFVGSTVRRYILDIMVHLRTHRLTYNAKAGGVYTNSLDDVVLLSRLIGLHSGKMFVSPSHVKEASRWYFPMHLELVQRSSMDSSLLYGSDPNLVDEMLEKLAKIKCEEVNEFENPLFLESLVVKNVLSKVVPPV
|
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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