entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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|---|---|---|---|---|
B5ZMW9
|
HRCA_RHILW
|
Heat-inducible transcription repressor HrcA
|
MGIRSTSVSDAVAALDERSREIFRRIVEGYLESGEPLGSRNLSRLLPMSLSPASVRNVMSDLEDLGLIYSPHISAGRLPTQIGLRFFVDAFMQVGDLSAEDRASIDRQVRAESGGNPVESMMNEASRMLSGISRGAGLVITSKSDPVLKHVEFIRLEPTKALAVLVGDHDQVENRIIELPAGVTSSQLAEAANFLNAHMSGQTLPELRKQLSQLKDNVRHELDALSRDLVERGIAVWAGSPDEGKPAQLIIRGRANLLEGLAGAEDLDRLRLLFDDLEKKDSLIEILNLAETGSGVRIFIGSENKLFSLSGSSLIVAPYRDDDDRIVGAVGVIGPTRLNYSRIVPMVDYTAQLVSRLSRNPL
|
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}.
|
B5ZRN9
|
NRDI_RHILW
|
Protein NrdI
|
MGLIVYYSSRSENTHRFVARLGLRAARIPAGGADAFHIREPFVLVVPTYSDGDGKGAVPKQVIRFLNDAENRGHIRGVIAAGNSNFGETYGLAGDVISQKCRVPYLYRFELIGTEEDVANVKHGMERFWTREQL
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B6EGG8
|
SYDP_ALISL
|
Protein Syd
|
MPLSVEQALANFSQRYVEAWKEKHDSLPINEELVGLASPCIDETRNLEVLWQPVARDESIRLVNIENGIELDLHDDFHAFYGAQFSADMTAKFEGMNVELLQIWSDEDLENLQGNMLGHLVMQRRLKLVPTLFIAVTDDEMEVISICNQSGEVILDTVGTKKRKVLAESMAEFLEKLEPVVA
|
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}.
|
B6EMT9
|
FETP_ALISL
|
Probable Fe(2+)-trafficking protein
|
MSRTVFCVLLNKEADGLDFQLYPGELGKRIFDNISKEAWGQWQHKQTMLINEKKLNMMDPEHRKMLETEMEGFLFDGKDVVIDGYTPPSK
|
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}.
|
B6HU36
|
LCL2_PENRW
|
Long chronological lifespan protein 2
|
MLQSWRQALWALLLLVSVAQAQFNFFDQMFGGGEQQRQQQRSQNSPSDSDRYQQMWNGAQCDHYLCPGTLACVHFPHHCPCPHPDVEEKVELGEGSAVCVSKGGFKAGEAARKIELARKGLL
|
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
|
B6HUQ5
|
ADRB_PENRW
|
Andrastin A biosynthesis cluster protein B
|
MQGWIVRISHWNTYLPIAGTMQACGDKSSVWKVAIGYNGHPEEATFFNGRRSYAVNNRGAKPEKERTLRLNIEITPVESQGCNQLPTPATFEFRIPHSHFFNWSVELYFHNAVLPSYRCHFCPRPSLVLRTHAISAEYSWLAVDITLGLNRHHNIAVEYVKYIKHLEVGKDIICQLLYLSGYFLYVVPLSIPTKYSKYVSQCTVDPYREAGGF
|
Part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the pathway having the andrastin scaffold, with the tetracyclic ring system (Ref.2). The post-cyclization tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the conversion of andrastin E into andrastin A. The short chain dehydrogenase adrF is responsible for the oxidation of the C-3 a hydroxyl group of andrastin E to yield the corresponding ketone, andrastin D. The ketoreductase adrE stereoselectively reduces the carbonyl moiety to reverse the stereochemistry of the C-3 position to yield andrastin F. The acetyltransferase adrJ is the acetyltransferase that attaches the acetyl group to the C-3 hydroxyl group of andrastin F to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA catalyzes two sequential oxidation reactions of the C-23 methyl group, to generate the corresponding alcohol andrastin B, and aldehyde andrastin A (Ref.2). {ECO:0000269|Ref.2}.
|
B6I2F4
|
LPMG_ECOSE
|
mgtA leader peptide (Regulatory leader peptide for mgtA)
|
MEPDPTPLPRRRLKLFR
|
Makes mgtA transcription sensitive to intracellular proline levels. Under low levels of proline this protein cannot be fully translated, and a stem loop forms which permits transcription of the downstream mgtA gene (By similarity).
|
B6I419
|
GLGS_ECOSE
|
Surface composition regulator
|
MDHSLNSLNNFDFLARSFARMHAEGRPVDILAVTGNMDEEHRTWFCARYAWYCQQMMQARELELEH
|
Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}.
|
B6I4N1
|
FDHE_ECOSE
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B6I665
|
NRDI_ECOSE
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B6I6J1
|
SYDP_ECOSE
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
|
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}.
|
B6I975
|
CBPM_ECOSE
|
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}.
|
B6IZY6
|
CBPM_COXB2
|
Chaperone modulatory protein CbpM
|
MTKQIIKGIIIERSSPLKIDELSQAVHLRREIIIEMVEHRLIEPEGSSPTSWKFDNVCLKRAKIAASFYRDLEINMPGIAIALDLLDKIEHLEQRLRTLERFENQE
|
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}.
|
B6J0C7
|
FETP_COXB2
|
Probable Fe(2+)-trafficking protein
|
MTRRIFCQKLGKEADALNYSPYPGELGERIYNHISEQAWQAWLSHQTMLINEYRLSLIDPKARQFLEQEMINFLFGTGSEKPAGYTSEKE
|
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}.
|
B6J775
|
FETP_COXB1
|
Probable Fe(2+)-trafficking protein
|
MTRRIICQKLGKEADALNYSPYPGELGERIYNHISEQAWQAWLSHQTMLINEYRLSLIDPKARQFLEQEMINFLFGTGSEKPAGYTSEKE
|
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}.
|
B6J7F6
|
CBPM_COXB1
|
Chaperone modulatory protein CbpM
|
MTKQIIKGIIIERSSPLKIDELSQAVHLRREIIIEMVEHRLIEPEGSSPTSWKFDNVCLKRAKIAASFYRDLEINMPGIAIALDLLDKIEHLEQRLRTLERFENQE
|
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}.
|
B6JNU6
|
YIDD_HELP2
|
Putative membrane protein insertion efficiency factor
|
MRNNKTPFLSAIFTASIRGYQRFFSAFTPSSCRFYPTCSNYALWLLYFESPLSAMGKIAIRILSCNPFCSGGIAYPVTRLKRPSLLQSHKDFNRNFKTITFWLVPTAKSRTTYYIIKV
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B6QFV5
|
LCL2_TALMQ
|
Long chronological lifespan protein 2
|
MLAKPLTAIWTLFLLISTAQAQFQFFEQMFGGGGSHQGHQQEQEASSDSSWYQQTWEGTHCTKYLCPDTLACVHFPHHCPCPHPSVEEKVELGEGSAVCVSRGGWTAGEAARKIELARKGVL
|
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
|
B7GFG2
|
YABA_ANOFW
|
Initiation-control protein YabA
|
MNKKEIFQSVTSIEEQIAHLYKQLGELKSYLGELIEENHRLQVENDHLRRRLEQLSERKVEQGKKQTKAKLVDIGEGYDNLARLYQEGFHICNVHYGSLRTDGDCLFCLSFLNKK
|
Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}.
|
B7GGE5
|
Y1766_ANOFW
|
UPF0122 protein Aflv_1766
|
MLEKTTRMNYLYDFYQSLLTPKQRNYMSLYYLDDYSLGEIAEEYEVSRQAVYDNIKRTEAMLEDYEQKLLLFQKFQQRHKLLHRLKTHIAERYPNDEELMKLVLELEKLE
|
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}.
|
B7GK26
|
YIDD_ANOFW
|
Putative membrane protein insertion efficiency factor
|
MKHIFILLIRFYQRFISPLKPPTCRFYPTCSHYGLEAIRRFGALKGGYLTIKRILKCHPFHPGGFDPVPEKEQK
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7GLD4
|
LUTC_ANOFW
|
Lactate utilization protein C
|
MEAFLQRIASRLGRDVRTSVERPQWKHAPQQTVFQGYSQNELLDVLKQQCTRIHTTFVETNSAELRDTLQQVIAAHGGGPIVVANDERYEQFGLSSFLQREDVYVWDATRGRDNIEAAERANIGMTWSDITLAESGTVVLLNNRDQGRTISFLPTTYVALIPKSTIVPRMTQAAHIIREKHVPSCINFITGPSNSADIEMNLVVGVHGPVKATYIVITDR
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02104}.
|
B7GLD6
|
LUTA_ANOFW
|
Lactate utilization protein A
|
MNVTLFVTCLVDLFHVNVGKATVELLERLGCTIHFPEAQTCCGQPAYNSGYVKEAKEAMKHMIRTFEHAEYIVTPSGSCATMFKEYPHIFKGDGEWEARAKRVADKTYELTQFIVDVLQVEDVGARLEGKATYHTSCHMTRLLGVKDAPLTLLQHVKGLEVVPLPNAHNCCGFGGTFSVKMGPISEQMVDEKIQCIEQVEADYLIGADCGCLMNIGGRIERKGKPIRVMHIAEVLNHR
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02105}.
|
B7GPF6
|
YIDD_BIFLS
|
Putative membrane protein insertion efficiency factor
|
MTASFKAVMIGGVRWYQQRISANTPPCCKYYPTCSNYAIEALERYGAFKGGVLAVLRLLRCRPWSRGGIDDVPQRYSIFYRFSWSKAHEEPRLTPLATTQREAQR
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7H341
|
YIDD_ACIB3
|
Putative membrane protein insertion efficiency factor
|
MVRILRWFIRLYQIAISPLLGPRCRYIPTCSQYALEALQTHGAIKGVWLSSKRICRCHPWGGSGYDPVPPKAIRFISFHQIDSQTHHVAVPFRDRLMKQNLSNHLG
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7H9G7
|
YIDD_BACC4
|
Putative membrane protein insertion efficiency factor
|
MKQIFIGIIRFYQKFISPMTPPTCRFYPTCSHYGLEAFQKHGAFKGFWLTCKRILKCHPFHPGGFDPVPDKKDDKVNS
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7HCU2
|
HRCA_BACC4
|
Heat-inducible transcription repressor HrcA
|
MLTERQLLILQTIIDDFIGSAQPVGSRTLAKKDEITFSSATIRNEMADLEELGFIEKTHSSSGRVPSEKGYRFYVDHLLAPQNLPNAEIVQIKDLFAERIFEAEKIAQQSAQILSELTNYTAIVLGPKLSTNKLKNVQIVPLDRQTAVAIIVTDTGHVQSKTITVPESVDLSDLEKMVNILNEKLSGVPMEELHNKIFKEIVTVLRGYVHNYDSAIKMLDGTFQVPLSEKIYFGGKANMLSQPEFHDIQKVRSLLTMIDNEAEFYDILRHKQVGIQVKIGRENSSTAMEDCSLISATYSIGEEQLGTIAILGPTRMQYSRVISLLQLFTRQFTDGLKK
|
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}.
|
B7HDW9
|
Y3945_BACC4
|
UPF0122 protein BCB4264_A3945
|
MLEKTTRMNYLFDFYQSLLTQKQRSYMSLYYLDDLSLGEIAEEFDVSRQAVYDNIKRTEAMLEEYEEKLVLLQKFQERQRLVAKLKQLISEEEHVNEEMKQVVEAIEKLD
|
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}.
|
B7HH58
|
LUTA_BACC4
|
Lactate utilization protein A
|
MKVTLFVTCLVDMFETNVGKATVEVLERLGCEIEFPEAQVCCGQPAYNSGHVEAAKEAMKHMIETFEDAEYIVTPSGSCATMFHEYPHVFKDDPKWAKRAQKVADKTYEFTQFIVDVLKVTDVGASLPGIATIHKSCHMTRMLGVKEAPGILLSNVKGLTVRDLPNVQNCCGFGGTFSVKMTPISEQMVDEKVDSVMETGADYLIGADCGCLLNIGGRIERLGKEVKVMHIAEVLNSRS
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02105}.
|
B7HH60
|
LUTC_BACC4
|
Lactate utilization protein C
|
MTGLIQNRDAFLDNIAKELGRARKTEGVERPVWKSNVNIETLKDYSQEELLEVFKKQCTNIHTTVVETTNDCLGEDLQKVIMENGGGPILLSADDRFDAYGLTSLFKEELPKRDVEVNVWDPERKDENMRLAEKANIGIAFSDYTLAESGTIVVQSHKGQGRSLHFLPTVYFAIIPRETLVPRITQAVQDMNSRVENGETAASCINFITGPSNSADIEMNLVVGVHGPLKAVYFIV
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02104}.
|
B7HLH9
|
Y3894_BACC7
|
UPF0122 protein BCAH187_A3894
|
MLEKTTRMNYLFDFYQSLLTQKQRSYMSLYYLDDLSLGEIAEEFDVSRQAVYDNIKRTEAMLEEYEEKLVLLQKFQERQRLVAKLKQLISEEEHVNEEMKQVVEAIEKLD
|
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}.
|
B7HPL5
|
HRCA_BACC7
|
Heat-inducible transcription repressor HrcA
|
MLTERQLLILQTIIDDFIGSAQPVGSRTLAKKDEITFSSATIRNEMADLEELGFIEKTHSSSGRVPSEKGYRFYVDHLLAPQNLPNDEIVQIKDLFAERIFEAEKIAQQSAQILSELTNYTAIVLGPKLSTNKLKNVQIVPLDRQTAVAIIVTDTGHVQSKTITVPESVDLSDLEKMVNILNEKLSGVPMSELHNKIFKEIVTVLRGYVHNYDSAIKILDGTFQVPLSEKIYFGGKANMLSQPEFHDIQKVRSLLTMIDNEAEFYDILRHKQVGIQVKIGRENSATAMEDCSLISATYSIGEEQLGTIAILGPTRMQYSRVISLLQLFTRQITDGLKK
|
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}.
|
B7HPU4
|
YABA_BACC7
|
Initiation-control protein YabA
|
MEKKDIFASVSSMEEQIGHLYKQLGELKQHLAELLEENQHIKMENENLRHRFEEVQIKEKQKTQKRKEVKPKTDIGEGYDNLARLYQEGFHICNLHYGSVRKEGDCLFCLSFLNKK
|
Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}.
|
B7HTQ3
|
YIDD_BACC7
|
Putative membrane protein insertion efficiency factor
|
MKQIFIGIIRFYQKFISPMTPPTCRFYPTCSHYGLEAFQKHGALKGFWLTCKRILKCHPFHPGGFDPVPDKKDDKVHS
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7I0K9
|
LUTA_BACC7
|
Lactate utilization protein A
|
MKVTLFVTCLVDMFETNVGKATVEVLERLGCEIEFPEAQVCCGQPAYNSGHVEAAKEAMKHMIETFEDAEYIVTPSGSCATMFHEYPHVFKDDPKWAKRAQKVADKTYEFTQFIVDVLKVTDVGASLPGIATIHKSCHMTRMLGVTEAPGILLSNVKGLTVRELPNVQNCCGFGGTFSVKMTPISEQMVDEKVDSAMETGADYLIGADCGCLLNIGGRIERLGKEIKVMHIAEVLNSRS
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02105}.
|
B7I0L1
|
LUTC_BACC7
|
Lactate utilization protein C
|
MTGLIQNRESFLENIAKELGRARKTDGVKRPVWKNNVNKETLKNYSQEELLEVFKNQCTNIHTTVVETTNDRLREDIQKVIVENGGGPIMLSADERFDSYGLTSLFKEELPKQNVEVNVWDPEKKEENMRIAERANIGIAFSDYTLAESGTIVVQSHKGQGRSLHFLPTVYLAIIPRETLVPRITQAVEDMNKRVENGETVASCINFITGPSNSADIEMNLVVGVHGPLKAVYFIV
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02104}.
|
B7I337
|
FETP_ACIB5
|
Probable Fe(2+)-trafficking protein
|
MSRQVFCRKYQKEMEGLDFAPFPGAKGQEFFENVSKQAWQEWLQHQTTLINEKRLNVFEPEAKKFLEEQREKFFNNDESVEKAEGWKPE
|
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}.
|
B7IBI0
|
YIDD_ACIB5
|
Putative membrane protein insertion efficiency factor
|
MVRILRWFIRLYQIAISPLLGPRCRYIPTCSQYALEALQTHGAIKGVWLSSKRICRCHPWGGSGYDPVPPKAIRFISFHQIDSQTHHVAVPFRDRLMKQNLSNHLG
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7ILV5
|
YIDD_BACC2
|
Putative membrane protein insertion efficiency factor
|
MKQIFIGIIRFYQKFISPMTPPTCRFYPTCSHYGLEAFQKHGALKGFWLTCKRILKCHPFHPGGFDPVPDKKDDKVNS
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7IMD3
|
LUTA_BACC2
|
Lactate utilization protein A
|
MKVTLFVTCLVDMFETNVGKATVEVLERLGCEIEFPEAQVCCGQPAYNSGHVEAAKEAMKHMIETFEDAEYIVTPSGSCATMFHEYPHVFKDDPKWAKRAQKVADKTYEFTQFIVDVLKVTDVGASLSGIATIHKSCHMTRMLGVKEAPGILLSNVKGLTVRDLPNVQNCCGFGGTFSVKMTPISEQMVDEKVDSVMETGADYLIGADCGCLLNIGGRIERLGKEVKVMHIAEVLNSRS
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02105}.
|
B7IMD5
|
LUTC_BACC2
|
Lactate utilization protein C
|
MTGLIQNRDAFLDNIAKELGRARKTEGVERPVWKSNVNIETLKDYSQEELLEVFKNQCTNIHTTVVETTNERLREDLQQVIMENGGGPILLSADERFDAYGLTSLFKEELPKRDVEVNVWDPERKDGNMRLAEKANIGIAFSDYTLAESGTIVVQSHKGQGRSLHFLPTVYLAIIPRETLVPRITQAVQDMNSRVEDGETAASCINFITGPSNSADIEMNLVVGVHGPLKAIYFIV
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02104}.
|
B7IUK5
|
Y1298_BACC2
|
UPF0122 protein BCG9842_B1298
|
MLEKTTRMNYLFDFYQSLLTQKQRSYMSLYYLDDLSLGEIAEEFDVSRQAVYDNIKRTEAMLEEYEEKLVLLQKFQERQRLVAKLKQLISEEEHVNEEMKQVVEAIEKLD
|
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}.
|
B7IYG9
|
HRCA_BACC2
|
Heat-inducible transcription repressor HrcA
|
MLTERQLLILQTIIDDFIGSAQPVGSRTLAKKDEITFSSATIRNEMADLEELGFIEKTHSSSGRVPSEKGYRFYVDHLLAPQNLPNAEIVQIKDLFAERIFEAEKIAQQSAQILSELTNYTAIVLGPKLSTNKLKNVQIVPLDRQTAVAIIVTDTGHVQSKTITVPESVDLSDLEKMVNVLNEKLSGVPMEELHNKIFKEIVTVLRGYVHNYDSAIRMLDGTFQVPLSEKIYFGGKANMLSQPEFHDIQKVRSLLTMIDNEAEFYDILRHKQVGIQVKIGRENTSTAMEDCSLISATYSIGEEQLGTIAILGPTRMQYSRVISLLQLFTRQFTDGLKK
|
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}.
|
B7J0N1
|
SP5G_BORBZ
|
Putative septation protein SpoVG
|
MDITDIRIKKVDSKNSGSKLLAYVAVTFDNCLVLHNIRVIKGQKGVFIAMPNRRTRVGEYKDIVHPISQDFRKALQTSIFKEYIRENPADLELELDF
|
Could be involved in septation. {ECO:0000255|HAMAP-Rule:MF_00819}.
|
B7J9T2
|
FETP_ACIF2
|
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}.
|
B7JF00
|
LUTA1_BACC0
|
Lactate utilization protein A 1
|
MKVTLFVTCLVDMFETNVGKATVEVLERLGCEIEFPEAQVCCGQPAYNSGHVEAAKEAMKHMIETFEDAEYIVTPSGSCATMFHEYPHVFKDDPKWAKRAQKVADKTYEFTQFIVDVLNVTDVGASLPGIATIHKSCHMTRMLGVTEAPGILLSNVKGLTVRELPNVQNCCGFGGTFSVKMTPISEQMVDEKVDSAMETGADYLIGADCGCLLNIGGRIERLGKEIKVMHIAEVLNSRS
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02105}.
|
B7JF02
|
LUTC_BACC0
|
Lactate utilization protein C
|
MTGLIQNRDSFLDNIAKELGRTRKTDGVERPVWKNNVNKETLKDYSQEELLEVFKNQCTNIHTTVVETTNDRLREDIQKVIVENGGGPIMLSADERFDSYGLTSLFKEELPKQNVEVNVWDPEKKEENMRIAERANIGIAFSDYTLAESGTIVVQSHKGQGRSLHFLPTVYFAIIPRETLVPRITQAVQDMNTRVENGEEVASCINFITGPSNSADIEMNLVVGVHGPLKAVYFIV
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02104}.
|
B7JF51
|
LUTA2_BACC0
|
Lactate utilization protein A 2
|
MKVSLFITCLSDVFFPQVGKSVVEIMNQCGVELDFPEGQTCCGQPAYNSGYQEDAKLAAKQMIKAFEHSEYIVTPSGSCASMVHHYYKEMFKGDSEWYEKAVHLADRTYELTDFLVNILGKNDWKSKLVEKAVFHQSCHMSRALGIKEEPLKLLSQVEGLDIKELPYCQDCCGFGGTFAVKMSSISETMVDEKIKHIEATEANLLIGADMGCLMNIGGRLRRENKNIQVLHVAEVLAKGLNK
|
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. {ECO:0000255|HAMAP-Rule:MF_02105}.
|
B7JJE4
|
YABA_BACC0
|
Initiation-control protein YabA
|
MEKKDIFASVSSMEEQIGHLYKQLGELKQHLAELLEENQHIKMENENLRHRFEEVQIKEKQKTQKRKEVKPKTDIGEGYDNLARLYQEGFHICNLHYGSVRKEGDCLFCLSFLNKK
|
Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}.
|
B7JJT3
|
Y3860_BACC0
|
UPF0122 protein BCAH820_3860
|
MLEKTTRMNYLFDFYQSLLTQKQRSYMSLYYLDDLSLGEIAEEFDVSRQAVYDNIKRTEAMLEEYEEKLVLLQKFQERQRLVAKLKQLISEEEHVNEEMKQVVEAIEKLD
|
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}.
|
B7JN41
|
HRCA_BACC0
|
Heat-inducible transcription repressor HrcA
|
MLTERQLLILQTIIDDFIGSAQPVGSRTLAKKDEITYSSATIRNEMADLEELGFIEKTHSSSGRVPSEKGYRFYVDHLLAPQNLPNDEIVQIKDLFAERIFEAEKIAQQSAQILSELTNYTAIVLGPKLSTNKLKNVQIVPLDRQTAVAIIVTDTGHVQSKTITVPESVDLSDLEKMVNILNEKLSGVPMSELHNKIFKEIVTVLRGYVHNYDSAIKMLDGTFQVPLSEKIYFGGKANMLSQPEFHDIHKVRSLLTMIDNEAEFYDILRHKQVGIQVKIGRENSATAMEDCSLISATYSIGEEQLGTIAILGPTRMQYSRVISLLQLFTRQFTDGLKK
|
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}.
|
B7JT58
|
YIDD_BACC0
|
Putative membrane protein insertion efficiency factor
|
MKQIFIGIIRFYQKFISPMTPPTCRFYPTCSHYGLEAFQKHGAFKGFWLTCKRILKCHPFHPGGFDPVPDKKDDKVNS
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7JWS8
|
YIDD_RIPO1
|
Putative membrane protein insertion efficiency factor
|
MKTLLIVLIKGYRNFISPLFPPSCRFQPTCSKYALEAVERFGVLHGGSLAIKRILRCHPFHPGGYDPVPLVDSSSKRSQ
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7K8P8
|
YIDD_GLOC7
|
Putative membrane protein insertion efficiency factor
|
MKIVLIGLIRGYRTFISPLFPPSCRFQPTCSQYGIEAIERFGAIKGAWLTLGRILRCHPFHPGGYDPVPPVKPKK
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
B7L848
|
YIDD_ECO55
|
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}.
|
B7L9E7
|
FDHE_ECO55
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B7LE91
|
NRDI_ECO55
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIAQKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B7LEX3
|
SYDP_ECO55
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
|
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}.
|
B7LFA8
|
CBPM_ECO55
|
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}.
|
B7LGY3
|
GLGS_ECO55
|
Surface composition regulator
|
MDHSLNSLNNFDFLARSFARMHAEGRPVDILAVTGNMDEEHRTWFCARYAWYCQQMMQARELELEH
|
Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}.
|
B7LK47
|
YIDD_ESCF3
|
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}.
|
B7LVF7
|
FDHE_ESCF3
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B7LVU6
|
SYDP_ESCF3
|
Protein Syd
|
MDELTAQALRDFTTRYCDAWHEKHHSWPLSEELYGVPSPCIISTTSDAVYWQPQPFVGEQNLAAVERAFDIVLQPAIQTFYTTQFAGDMHAQFAEHTLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLSPTLFIATLENELDVISLCNLSGEVCKETLGTRNRQVLAPSLAEFLKQLNPLL
|
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}.
|
B7LW06
|
NRDI_ESCF3
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B7LXK9
|
SYDP_ECO8A
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
|
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}.
|
B7LZJ8
|
GLGS_ECO8A
|
Surface composition regulator
|
MDHSLNSLNNFDFLARSFARMHAEGRPVDILAVTGNMDEEHRTWFCARYAWYCQQMMQARELELEH
|
Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}.
|
B7M557
|
YIDD_ECO8A
|
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}.
|
B7M693
|
FDHE_ECO8A
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B7M8Y2
|
CBPM_ECO8A
|
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}.
|
B7M9B7
|
NRDI_ECO8A
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIAQKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B7MAC5
|
GLGS_ECO45
|
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}.
|
B7MGC6
|
YIDD_ECO45
|
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}.
|
B7MI25
|
FDHE_ECO45
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTTRIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B7MIE5
|
CBPM_ECO45
|
Chaperone modulatory protein CbpM
|
MANVTVTFTITEFCLHTGISEEELNEIVGLGVVEPSEIQETTWVFDDHAAIVVQRAVRLRHELALDWPGIAVALTLMDDIAHLKQENRLLRQRLSRFVAHP
|
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}.
|
B7MKE7
|
NRDI_ECO45
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCSVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B7MLB4
|
SYDP_ECO45
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
|
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}.
|
B7MPT1
|
CBPM_ECO81
|
Chaperone modulatory protein CbpM
|
MANVTVTFTITEFCLHTGISEEELNEIVGLGVVEPSEIQETTWVFDDHAAIVVQRAVRLRHELALDWPGIAVALTLMDDIAHLKQENRLLRQRLSRFVAHP
|
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}.
|
B7MQY5
|
FDHE_ECO81
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTTRIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B7MYX8
|
NRDI_ECO81
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B7MZ89
|
SYDP_ECO81
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAIYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
|
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}.
|
B7N052
|
GLGS_ECO81
|
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}.
|
B7N2F0
|
YIDD_ECO81
|
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}.
|
B7N3F4
|
CBPM_ECOLU
|
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}.
|
B7N6R0
|
NRDI_ECOLU
|
Protein NrdI
|
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRVLLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQP
|
Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
|
B7N727
|
SYDP_ECOLU
|
Protein Syd
|
MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRAHLASNLAEFLNQLKPLL
|
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}.
|
B7ND37
|
GLGS_ECOLU
|
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}.
|
B7NF22
|
YIDD_ECOLU
|
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}.
|
B7NFJ2
|
FDHE_ECOLU
|
Protein FdhE
|
MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTTRIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
|
Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
|
B7NJR2
|
GLGS_ECO7I
|
Surface composition regulator
|
MDHSLNSLNNFDFLARSFARMHAEGRPVDILAVTGNMDEEHRTWFCARYAWYCQQMMQARELELEH
|
Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}.
|
B7NLC6
|
CBPM_ECO7I
|
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}.
|
B7NR07
|
YIDD_ECO7I
|
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}.
|
B7NSF9
|
NRDI_ECO7I
|
Protein NrdI
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MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTTGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
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Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
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B7NUB8
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FDHE_ECO7I
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Protein FdhE
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MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTTRIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLHCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
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Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
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B7NVU1
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SYDP_ECO7I
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Protein Syd
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MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
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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}.
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B7UH94
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NRDI_ECO27
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Protein NrdI
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MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRPVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIAQKCGVPWLYSFELMGTQSDIENVRKGVTEFWQRQPQNA
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Probably involved in ribonucleotide reductase function. {ECO:0000255|HAMAP-Rule:MF_00128}.
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B7UHK9
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SYDP_ECO27
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Protein Syd
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MDDLTAQALKDFTARYCDAWHEEHKSWPLSEELYGVPSPCIISTTEDAVYWQPQPFTGEQNVNAVERAFDIVIQPTIHTFYTTQFAGDMHAQFGDIKLTLLQTWSEDDFRRVQENLIGHLVTQKRLKLPPTLFIATLEEELEVISVCNLSGEVCKETLGTRKRTHLASNLAEFLNQLKPLL
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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}.
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B7UIV7
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GLGS_ECO27
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Surface composition regulator
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MDHSLNSLNNFDFLARSFARMHAEGRPVDILAVTGNMDEEHRTWFCARYAWYCQQMMQTRELELEH
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Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides. {ECO:0000255|HAMAP-Rule:MF_00525}.
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B7UNL0
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FDHE_ECO27
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Protein FdhE
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MSIRIIPQDELGSSEKRTADMIPPLLFPRLKNLYNRRAERLRELAENNPLGDYLRFAALIAHAQEVVLYDHPLEMDLTARIKEASAQGKPPLDIHVLPRDKHWQKLLMALIAELKPEMSGPALAVIENLEKASTQELEDMASALFASDFSSVSSDKAPFIWAALSLYWAQMANLIPGKARAEYGEQRQYCPVCGSMPVSSMVQIGTTQGLRYLRCNLCETEWHVVRVKCSNCEQSGKLHYWSLDDEQAAIKAESCDDCGTYLKILYQEKEPKVEAVADDLASLVLDARMEQEGYARSSINPFLFPGEGE
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Necessary for formate dehydrogenase activity. {ECO:0000255|HAMAP-Rule:MF_00611}.
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B7V3P2
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FETP_PSEA8
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Probable Fe(2+)-trafficking protein
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MSRTVMCRKYHEELPGLDRPPYPGAKGEDIYNNVSRKAWDEWQKHQTMLINERRLNMMNAEDRKFLQQEMDKFLSGEDYAKADGYVPPSA
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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}.
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B7VA59
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YIDD_PSEA8
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Putative membrane protein insertion efficiency factor
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MKFLLIGLIRFYQYAISPLIGPRCRFYPSCSHYTLEAIRVHGALRGGYLGARRLLRCHPWHPGGYDPVPERQEQACACHRTAKPGK
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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