ID   RAVA_SALG2              Reviewed;         498 AA.
AC   B5RFU9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=SG3554;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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; AM933173; CAR39343.1; -; Genomic_DNA.
DR   RefSeq; WP_000940970.1; NC_011274.1.
DR   AlphaFoldDB; B5RFU9; -.
DR   SMR; B5RFU9; -.
DR   EnsemblBacteria; CAR39343; CAR39343; SG3554.
DR   KEGG; seg:SG3554; -.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   Proteomes; UP000008321; 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_1000186132"
SQ   SEQUENCE   498 AA;  56689 MW;  4ADEAC79C3B661AE CRC64;
     MAHPHLLAER ISRLSCALEK GLYERSHAIR LCLLAALSGE SVFLLGPPGI AKSLIARRLK
     FAFQRARAFE YLMTRFSTPE EVFGPLSIQA LKDEGRYERL TTGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERHFRNGA FEEKIPMRLL VAASNELPEA DSSLEALYDR MLIRLWLDKV
     QDKANFRSML VSQQDESDNP VPASLQVSDE EYQQWQKDIG AISLPDPVFE LIFTLRQQLD
     NLPNAPYVSD RRWKKAIRLL QASAFFSGRD AVAPIDLILL KDCLWYDAQS LNLMQQQLEI
     LMTGHAWQQQ AMLTRLGGIV QRRLQLQQQQ SDKTAFTVIK EGGMFSRRPH YTLPPEASAS
     TLTLLLQKPL KLHDMEVIHI TFDRSALELW LTKGGEIRGK LNGIGFAQTL NMEVDNAQHL
     VVRDISLQGT RLALPGAAED SMPAEIKQQL ETLENDWRQQ HTRFSEQQHC LFIHSDWLGR
     IEASLQDVGE QIRQAQQC