ID   RAVA_SALTY              Reviewed;         498 AA.
AC   Q8ZKW2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=STM3879;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL22737.1; -; Genomic_DNA.
DR   RefSeq; NP_462778.1; NC_003197.2.
DR   RefSeq; WP_000940991.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZKW2; -.
DR   SMR; Q8ZKW2; -.
DR   STRING; 99287.STM3879; -.
DR   PaxDb; Q8ZKW2; -.
DR   EnsemblBacteria; AAL22737; AAL22737; STM3879.
DR   GeneID; 1255406; -.
DR   KEGG; stm:STM3879; -.
DR   PATRIC; fig|99287.12.peg.4109; -.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   PhylomeDB; Q8ZKW2; -.
DR   BioCyc; SENT99287:STM3879-MON; -.
DR   Proteomes; UP000001014; 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; Reference proteome.
FT   CHAIN           1..498
FT                   /note="ATPase RavA"
FT                   /id="PRO_0000209377"
SQ   SEQUENCE   498 AA;  56703 MW;  D8DE2BFDFF4A1092 CRC64;
     MAHPHLLAER ISRLSSALEK 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 RLALPGTAED SMPAEIKQQL ETLENDWRQQ HTRFSEQQHC LFIHSDWLGR
     IEASLQDVGE QIRQAKQC