ID   RAVA_ECOSM              Reviewed;         498 AA.
AC   B1LL73;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=EcSMS35_4114;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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; CP000970; ACB15582.1; -; Genomic_DNA.
DR   RefSeq; WP_012311586.1; NC_010498.1.
DR   AlphaFoldDB; B1LL73; -.
DR   SMR; B1LL73; -.
DR   EnsemblBacteria; ACB15582; ACB15582; EcSMS35_4114.
DR   KEGG; ecm:EcSMS35_4114; -.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   Proteomes; UP000007011; 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_1000186129"
SQ   SEQUENCE   498 AA;  56449 MW;  81AB5E33CA358689 CRC64;
     MAHPHLLAER ISRLSSSLEK GLYERSHAIR LCLLAALSGE SVFLLGPPGI AKSLIARRLK
     FAFQNARAFE YLMTRFSTPE EVFGPLSIQA LKDEGRYERL TSGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERQFRNGA HIEKIPMRLL VAASNELPEA DSSLEALYDR MLIRLWLDKV
     QDKANFRSML TSQQDENDNP VPTSLQVTDE EYERWQKEIG EITLPDHVFE LIFMLRQQLD
     KLPDAPYVSD RRWKKAIRLL QASAFFSGRS AVAPVDLILL KDCLWYDAQS LNLIQQQIDV
     LMTGHAWQQQ GMLTRLGAIV QRHLQLQQQQ SDKTALTVIR LGGIFSRRQQ YQLPVNVTAS
     TLTLLLQKPL KLHDMEVVHI TFERSALEQW LSKGGEIRGK LNGIGFAQKL NLEVDSTQHL
     VVRDVSLQGS TLALPGSSAE GLPGEIKQQL EELESDWRKQ HALFSEQQKC LFIPGDWLGR
     IEASLQDVGA QIRQAQQC