ID   RAVA_YERPS              Reviewed;         512 AA.
AC   Q66GH6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=YPTB0005;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19245.1; -; Genomic_DNA.
DR   RefSeq; WP_011191439.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66GH6; -.
DR   SMR; Q66GH6; -.
DR   EnsemblBacteria; CAH19245; CAH19245; YPTB0005.
DR   GeneID; 66843603; -.
DR   KEGG; ypo:BZ17_2594; -.
DR   KEGG; yps:YPTB0005; -.
DR   PATRIC; fig|273123.14.peg.2720; -.
DR   OMA; HANAFEY; -.
DR   Proteomes; UP000001011; 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..512
FT                   /note="ATPase RavA"
FT                   /id="PRO_0000209383"
SQ   SEQUENCE   512 AA;  58731 MW;  FA4F9B1CC920CDEF CRC64;
     MAQSSQLAER ISRLSHALES GLYERQEAIR LCLLAALSGE SVFLLGPPGI AKSLIARRLK
     FAFRHARAFE YLMTRFSTPE EVFGPLSIQA LKEEGRYQRM TGGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERRFRNGD REDSIPMRLL VTASNELPDA DSSLEALYDR MLIRLWLDRV
     QEKQNFRSLL ISRQNENHNP VAENLSITDE EFHQWQPLID KITLPDHCFE LIFQLRQRLS
     ALEHAPYVSD RRWKKALRLL QASAFFSGRD EITPIDLILL KDCLWHDLNS FKLLQQQLEQ
     LLTEQGYQQQ SLLMKLQDIN SKWLQHQQQQ SDHQALTVVK QSGMFSRKAQ YALPDNLTDS
     TLTLLLQKPL NLHDIQVNHL QVDKEALAQW LNKGGALRAK LNGVGYAQSI DAEIDDQLHI
     IILDVSRQPS TLSLPGATTT SVPPELLLAL TKLESTLAEQ RRLFSQHQPC LFTPSSWLAK
     IEASLLQVVE QLQFQQIQFQ QRKFQQQKHS GH