ID   RAVA_SHIDS              Reviewed;         498 AA.
AC   Q329T5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 85.
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=SDY_4002;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB63920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000034; ABB63920.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005016794.1; NC_007606.1.
DR   RefSeq; YP_405411.2; NC_007606.1.
DR   AlphaFoldDB; Q329T5; -.
DR   SMR; Q329T5; -.
DR   STRING; 300267.SDY_4002; -.
DR   EnsemblBacteria; ABB63920; ABB63920; SDY_4002.
DR   KEGG; sdy:SDY_4002; -.
DR   PATRIC; fig|300267.13.peg.4714; -.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   Proteomes; UP000002716; 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_0000209379"
SQ   SEQUENCE   498 AA;  56496 MW;  24D4D6A749969C81 CRC64;
     MAHPHLLAER ISRLSSSLEK GLYERSHAIR LCLLAALSGE SMFLLGPPGI AKSLIARRLK
     FAFQNARAFE YLMTRFSTPE EVFGPLSIQA LKDEGRYERL TSGYLPEAEI VFLDEIWKAG
     PAILNTLLTA INERQFRNGA HVEKIPMRLL VAASNELPEA DSSLEALYDR MLIRLWLDKV
     QDKANFRSML TSQQDENDNP VPDALQVTDE EYERWQKEIG EITLPDHVFE LIFMLRQQLD
     KLPDAPYVSD RRWKKAIRLL QASAFFSGRS AVAPVDLILL KDCLWYDAQS LNLIQQQIDV
     LMTGHAWQQQ GMLTRLGAIV QRHLQLQQQQ SDKTALTVIR LGGIFSRRQQ YQLPVNVTAS
     TLTLLLQKPL KLHDMEVVHI SFERSALEQW LSKGGEIRGK LNGIGFAQKL NLEVDSAQHL
     VVRDVSLQGS TLALPGSSAE SMPGKIKQQL EELESDWRKQ HALFSEQQRC LFIPGDWLGR
     IEASLQDVGA QIRQAQQC