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 27-MAR-2024, entry version 114.
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; Pseudomonadota; 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; 99287-STM3879; -.
DR GeneID; 1255406; -.
DR KEGG; stm:STM3879; -.
DR PATRIC; fig|99287.12.peg.4109; -.
DR HOGENOM; CLU_018678_1_0_6; -.
DR PhylomeDB; Q8ZKW2; -.
DR BioCyc; SENT99287:STM3879-MONOMER; -.
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 CDD; cd00009; AAA; 1.
DR Gene3D; 1.20.58.1510; -; 1.
DR Gene3D; 2.40.128.430; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR046898; RavA_LARA_dom.
DR InterPro; IPR046932; RavA_LARA_sf.
DR PANTHER; PTHR32204; ATPASE RAVA; 1.
DR PANTHER; PTHR32204:SF0; ATPASE RAVA; 1.
DR Pfam; PF17868; AAA_lid_8; 1.
DR Pfam; PF12592; ATPase_RavA_C; 1.
DR Pfam; PF20030; bpMoxR; 1.
DR Pfam; PF20265; LARA_dom; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
