ID   RAVA_ECOLC              Reviewed;         498 AA.
AC   B1IWZ2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-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}; OrderedLocusNames=EcolC_4248;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79844.1; -; Genomic_DNA.
DR   RefSeq; WP_001300947.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IWZ2; -.
DR   SMR; B1IWZ2; -.
DR   PRIDE; B1IWZ2; -.
DR   KEGG; ecl:EcolC_4248; -.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
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_1000088097"
SQ   SEQUENCE   498 AA;  56446 MW;  5D360AF7A1FF664B 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
     IEASLQDVSA QIRQAQQC