ID   RAVA_ECO24              Reviewed;         498 AA.
AC   A7ZTV7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=ATPase RavA {ECO:0000255|HAMAP-Rule:MF_01625};
DE            EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01625};
DE   AltName: Full=Regulatory ATPase variant A {ECO:0000255|HAMAP-Rule:MF_01625};
GN   Name=ravA {ECO:0000255|HAMAP-Rule:MF_01625};
GN   OrderedLocusNames=EcE24377A_4262;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Functions as an ATPase. May play a role in metal insertion
CC       (metal-chelatase) or as a chaperone. {ECO:0000255|HAMAP-Rule:MF_01625}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01625}.
CC   -!- SIMILARITY: Belongs to the RavA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01625}.
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DR   EMBL; CP000800; ABV19557.1; -; Genomic_DNA.
DR   RefSeq; WP_001315921.1; NC_009801.1.
DR   AlphaFoldDB; A7ZTV7; -.
DR   SMR; A7ZTV7; -.
DR   EnsemblBacteria; ABV19557; ABV19557; EcE24377A_4262.
DR   GeneID; 66672350; -.
DR   KEGG; ecw:EcE24377A_4262; -.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01625; ATPase_RavA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR023671; ATPase_RavA.
DR   InterPro; IPR022547; ATPase_RavA_C.
DR   InterPro; IPR045427; MoxR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041538; RavA-like_AAA_lid.
DR   Pfam; PF17868; AAA_lid_8; 1.
DR   Pfam; PF20030; bpMoxR; 1.
DR   Pfam; PF12592; DUF3763; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..498
FT                   /note="ATPase RavA"
FT                   /id="PRO_1000069601"
SQ   SEQUENCE   498 AA;  56416 MW;  5D274EF7A1FF664B CRC64;
     MAHPHLLAER ISRLSSSLEK GLYERSHAIR LCLLAALSGE SVFLLGPPGI AKSLIARRLK
     FAFQNARAFE YLMTRFSTPE EVFGPLSIQA LKDEGRYERL TSGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERQFRNGA HVEKIPMRLL VAASNELPEA DSSLEALYDR MLIRLWLDKV
     QDKANFRSML TSQQDENDNP VPDALQVTDE EYERWQKEIG EITLPDHVFE LIFMLRQQLD
     KLPDAPYVSD RRWKKAIRLL QASAFFSGRS AVAPVDLILL KDCLWYDAQS LNLIQQQIDV
     LMTGHAWQQQ GMLTRLGAIV QRHLQLQQQQ SDKTALTVIR LGGIFSRRQQ YQLPVNVTAS
     TLTLLLQKPL KLHDMEVVHI SFERNALEQW LSKGGEIRGK LNGIGFAQKL NLEVDSAQHL
     VVRDVSLQGS TLALPGSSAE GLPGEIKQQL EELESDWRKQ HALFSEQQKC LFIPGDWLGR
     IEASLQDVGA QIRQAQQC