RAVA_YERPG
ID RAVA_YERPG Reviewed; 512 AA.
AC A9QYG5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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};
GN OrderedLocusNames=YpAngola_A0005;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX86752.1; -; Genomic_DNA.
DR RefSeq; WP_012228846.1; NZ_CP009935.1.
DR AlphaFoldDB; A9QYG5; -.
DR SMR; A9QYG5; -.
DR KEGG; ypg:YpAngola_A0005; -.
DR PATRIC; fig|349746.12.peg.953; -.
DR OMA; HANAFEY; -.
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_1000186138"
SQ SEQUENCE 512 AA; 58788 MW; EF6F420E7F8014FD 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
ALEHTPYVSD RRWKKALRLL QASAFFSGRD EITPIDLILL KDCLWHDLNS FKLLQQQLEQ
LLTEQGYQQQ NLLMKLQDIN SKWLQHQQQQ SDHQALTVVK QSGMFSRKAQ YALPDNLTDS
TLTLLLQKPL NLHDIQVNHL QVDKEALAQW LNKGGALRAK LNGVGYAQSI DAEIDDQLHI
IILDVSRQPS TLSLPGATTT SVPPELLLAL TKLESTLAEQ RRLFSQHQPC LFTPSSWLAK
IEASLLQVVE QLQFQQIQFQ QRKFQQQKHS GH