{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P31473","secondaryAccessions":["Q2M864"],"uniProtkbId":"RAVA_ECOLI","entryAudit":{"firstPublicDate":"1993-07-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-07-15","entryVersion":182,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Regulatory ATPase RavA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31992852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"3.6.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16301313"}],"value":"Regulatory ATPase variant A"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16301313"}],"value":"ravA"},"synonyms":[{"value":"yieN"}],"orderedLocusNames":[{"value":"b3746"},{"value":"JW3725"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24454883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31992852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36625597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21148420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24454883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27080013"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36625597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31992852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31992852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"ATPase activity is stimulated by ViaA (PubMed:16301313, PubMed:27979649, PubMed:37660904). ATPase activity is also stimulated by interaction with the inducible lysine decarboxylase CadA/LdcI at low pH (PubMed:16301313, PubMed:31992852). The complex formed with CadA/LdcI represents a possible means of regulating RavA activity in response to acid stress conditions (PubMed:16301313). CadA/LdcI may stabilize RavA oligomers under acid stress conditions (PubMed:16301313)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":790.0,"unit":"uM","substrate":"ATP (at pH 7.5)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"}],"value":"kcat is 1.4 sec(-1) with ATP as substrate (at pH 7.5)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"}],"value":"Optimum pH is 7.5 for ATPase activity."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21148420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24454883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25097238"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27080013"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31992852"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"Homohexamer (PubMed:16301313, PubMed:21148420, PubMed:25097238, PubMed:31992852). Interacts with ViaA (PubMed:16301313, PubMed:27979649, PubMed:36127320, PubMed:37660904). Interacts with specific subunits of the NADH-quinone oxidoreductase complex (NDH-1 or Nuo complex), particularly with NuoA and NuoF under aerobic conditions, and with the fused NuoCD under anaerobic conditions (PubMed:24454883). Interacts strongly with the inducible lysine decarboxylase CadA/LdcI, forming a large cage-like structure composed of two CadA/LdcI decamers and five RavA hexamers (PubMed:16301313, PubMed:21148420, PubMed:25097238, PubMed:27080013, PubMed:31992852). Does not interact with the constitutive lysine decarboxylase LdcC (PubMed:16301313). Interactions with ViaA or CadA/LdcI and phosphatidylglycerol are mutually exclusive (PubMed:36127320)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P31473","intActId":"EBI-561223"},"interactantTwo":{"uniProtKBAccession":"P0A9H3","geneName":"cadA","intActId":"EBI-545922"},"numberOfExperiments":13,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P31473","intActId":"EBI-561223"},"interactantTwo":{"uniProtKBAccession":"P31473","geneName":"ravA","intActId":"EBI-561223"},"numberOfExperiments":7,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"}],"value":"Localizes to the membrane via interaction with specific lipids"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24454883"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36127320"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301313"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27979649"}],"value":"Part of the ravA-viaA operon, which is under the direct control of sigma S in aerobically grown cells (PubMed:16301313). In cells grown under oxygen-limiting conditions, expression is largely dependent on the anaerobic transcriptional regulator Fnr (PubMed:27979649). The operon is coexpressed with multiple anaerobic respiratory genes, many of which are regulated by Fnr (PubMed:27979649). Levels increase toward late log/early stationary phase (PubMed:16301313)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21148420"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"A protomer can be divided into three domains: the N-terminal domain is the AAA+ module, which is composed of two subdomains, the alpha-beta-alpha subdomain and the all-alpha subdomain (PubMed:21148420). The second domain is a discontinuous triple-helical domain (PubMed:21148420, PubMed:37660904). The third domain, named the LARA domain, contains a compact antiparallel beta-barrel-like domain forming a unique fold (PubMed:21148420, PubMed:37660904). Binding between ViaA and the triple-helical bundle domain of RavA results in the enhancement of the ATPase activity of RavA (PubMed:37660904). The LARA domain mediates RavA-CadA/LdcI interactions (PubMed:21148420)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37660904"}],"value":"The double ravA-viaA deletion mutant shows increased persistence when grown in the presence of fumarate and kanamycin"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01625"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the RavA family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAA62099.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"Regulatory ATPase 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