ID   RAVA_YERE8              Reviewed;         502 AA.
AC   A1JHR5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-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}; OrderedLocusNames=YE0006;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL10151.1; -; Genomic_DNA.
DR   RefSeq; WP_011815252.1; NC_008800.1.
DR   RefSeq; YP_001004403.1; NC_008800.1.
DR   AlphaFoldDB; A1JHR5; -.
DR   SMR; A1JHR5; -.
DR   STRING; 393305.YE0006; -.
DR   EnsemblBacteria; CAL10151; CAL10151; YE0006.
DR   KEGG; yen:YE0006; -.
DR   PATRIC; fig|393305.7.peg.95; -.
DR   eggNOG; COG0714; Bacteria.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   Proteomes; UP000000642; 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..502
FT                   /note="ATPase RavA"
FT                   /id="PRO_0000292353"
SQ   SEQUENCE   502 AA;  57374 MW;  2CE5EA709BB3179D CRC64;
     MAQSSQLAER ISRLSSALES GLYERQEAIR LCLLAALSGE SVFLLGPPGI AKSLIARRLK
     FAFRNARAFE YLMTRFSTPE EVFGPLSIQA LKEEGRYQRM TGGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERRFRNGD REDSIPMRLL VTASNELPDA DSSLEALYDR MLIRLWLDRV
     QEKQNFRSLL LSRQNENHNP VAENLSISDE EFYQWQPLID KIALPDNCFE LIFQLRQQLS
     AQEQAPYVSD RRWKKALRLL QASAFFSGRD EITPIDLILL KDCLWHDLSS LKLLQQQLEQ
     LLTEHGYQQQ SLLMKLQHIH AQWLKHQQQQ SDHQALTVTK QSGMFSRKPQ YSLPDHLTDS
     TLTLFLQKPL SLHDIQVNHL QIEKEMLVQW LNKGGVLRAK LNGVGYAQSI DAEVDDQLHI
     TVLDVSRQSS ILSQPGASTA SVPPELLVEL AELENSLAEQ RRLFSQHQPC LFTPSSWLAK
     IEASLLNVAE QVKQLQQKLR GH