ID   RAVA_PECCP              Reviewed;         499 AA.
AC   C6DJF8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=PC1_4243;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT15257.1; -; Genomic_DNA.
DR   RefSeq; WP_015842322.1; NC_012917.1.
DR   AlphaFoldDB; C6DJF8; -.
DR   SMR; C6DJF8; -.
DR   STRING; 561230.PC1_4243; -.
DR   EnsemblBacteria; ACT15257; ACT15257; PC1_4243.
DR   KEGG; pct:PC1_4243; -.
DR   eggNOG; COG0714; Bacteria.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   OrthoDB; 895310at2; -.
DR   Proteomes; UP000002736; 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..499
FT                   /note="ATPase RavA"
FT                   /id="PRO_1000215744"
SQ   SEQUENCE   499 AA;  57564 MW;  BE97F559AA9B59AF CRC64;
     MRQTAALAER ISRLSHALEH GLYERQHAIR LCLLAALSGE SVFLLGPPGI AKSMIARRLK
     FAFRHANAFE YLMTRFSTPE EVFGPLSIQA LKDEGRYQRL TAGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERRFRNGN SEDTIPMRLL VAASNELPEA DGGLEALYDR MLIRLWLDRV
     QEKQNFRALL VNNSSERDNP VPPALSVSDE EYQQWQKDIE HIALPEAGFE LIYTLRQQLD
     ALEQAPYISD RRWKKALRLL QASAFFCGRD TITPVDIILL KDCLWHDQST LTLIEHQLEL
     LITEHAYQQK SLLFRLQQVN TKRQQYQREQ SELQAFSVEK QGHFLGRKFH YALPDTIDTE
     TLELVLQRPL ILHDIEVNHL IIDKNALQGW LQKGGEIRGK LNGIGFTQRL DLLVDDRQHL
     AIRDISLQSS ILSLPEKRDI ALPAEITDEY EKLNMQLREQ RRLFSQHQPC LFVPSEWLAK
     IEASLQQVAE QIQQSEQQD