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{
"metadata": {
"accession": "P31473",
"id": "RAVA_ECOLI",
"source_organism": {
"taxId": "83333",
"scientificName": "Escherichia coli (strain K12)",
"fullName": "Escherichia coli (strain K12)"
},
"name": "Regulatory ATPase RavA",
"description": [
"Component of the RavA-ViaA chaperone complex, which may act on the membrane to optimize the function of some of the respiratory chains (PubMed:16301313, PubMed:24454883, PubMed:27979649, PubMed:36127320, PubMed:36625597). RavA functions as an ATPase (PubMed:16301313, PubMed:27979649, PubMed:31992852, PubMed:37660904)",
"The RavA-ViaA system is involved in the regulation of two respiratory complexes, the fumarate reductase (Frd) electron transport complex and the NADH-quinone oxidoreductase complex (NDH-1 or Nuo complex) (PubMed:24454883, PubMed:27979649). It modulates the activity of the Frd complex, signifying a potential regulatory function during bacterial anaerobic respiration with fumarate as the terminal electron acceptor (PubMed:27979649). Interaction of RavA-ViaA with FrdA results in a decrease in Frd activity (PubMed:27979649). It also interacts with the Nuo complex, known to be involved in both the aerobic and the anaerobic respiration (PubMed:24454883). The RavA-ViaA system binds to specific membrane phospholipids, and might chaperone certain respiratory complexes by acting on lipid microdomains in which these complexes are inserted (PubMed:36127320). The RavA-ViaA system also plays a negative role in bacterial persistence upon treatment with antibiotics through the association of the chaperone complex with Frd (PubMed:37660904). It sensitizes cells to sublethal concentrations of aminoglycoside (AG) antibiotics (PubMed:36127320, PubMed:36625597, PubMed:37660904). The system can facilitate uptake of AG across the membrane when cells are in a low energy state (PubMed:36625597). It sensitizes cells to AG through a proton motive force-dependent mechanism (PubMed:36127320, PubMed:36625597). Under fumarate respiration conditions, it sensitizes cells to AG via a FrdA-dependent mechanism (PubMed:36625597). It does not sensitize cells grown under nitrate respiration to gentamicin (PubMed:36625597). In addition, RavA is involved in the bacterial acid stress response (PubMed:27080013). Acts by binding to the inducible lysine decarboxylase CadA/LdcI, a key enzyme in the acid stress response, which reduces binding of CadA/LdcI to its potent inhibitor, the stringent response alarmone ppGpp, and thus modulates CadA/LdcI activity (PubMed:21148420, PubMed:27080013). RavA also has GTPase activity in vitro (PubMed:16301313). GTP hydrolysis is much slower than ATP hydrolysis at lower enzyme/substrate concentrations but reaches comparable levels with increasing amounts of enzyme/substrate (PubMed:16301313)"
],
"length": 498,
"sequence": "MAHPHLLAERISRLSSSLEKGLYERSHAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFQNARAFEYLMTRFSTPEEVFGPLSIQALKDEGRYERLTSGYLPEAEIVFLDEIWKAGPAILNTLLTAINERQFRNGAHVEKIPMRLLVAASNELPEADSSLEALYDRMLIRLWLDKVQDKANFRSMLTSQQDENDNPVPDALQVTDEEYERWQKEIGEITLPDHVFELIFMLRQQLDKLPDAPYVSDRRWKKAIRLLQASAFFSGRSAVAPVDLILLKDCLWYDAQSLNLIQQQIDVLMTGHAWQQQGMLTRLGAIVQRHLQLQQQQSDKTALTVIRLGGIFSRRQQYQLPVNVTASTLTLLLQKPLKLHDMEVVHISFERSALEQWLSKGGEIRGKLNGIGFAQKLNLEVDSAQHLVVRDVSLQGSTLALPGSSAEGLPGEIKQQLEELESDWRKQHALFSEQQKCLFIPGDWLGRIEASLQDVGAQIRQAQQC",
"proteome": "UP000000625",
"gene": "ravA",
"go_terms": [
{
"identifier": "GO:0016887",
"name": "ATP hydrolysis activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0005737",
"name": "cytoplasm",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"protein_evidence": 1,
"source_database": "reviewed",
"is_fragment": false,
"in_alphafold": true,
"in_bfvd": false,
"ida_accession": "1e61583faf737e15ed7fb136c5d5fa3fc3f00e32",
"counters": {
"domain_architectures": 1785,
"entries": 22,
"isoforms": 0,
"proteomes": 1,
"sets": 3,
"structures": 8,
"taxa": 1,
"dbEntries": {
"cathgene3d": 3,
"pfam": 4,
"ssf": 1,
"cdd": 1,
"smart": 1,
"hamap": 1,
"ncbifam": 1,
"panther": 1,
"interpro": 9
},
"proteome": 1,
"taxonomy": 1,
"similar_proteins": 1785
}
}
}
