RAVA_ECOBW
ID RAVA_ECOBW Reviewed; 498 AA.
AC C4ZZ24;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=BWG_3437;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR63238.1; -; Genomic_DNA.
DR RefSeq; WP_001299914.1; NC_012759.1.
DR AlphaFoldDB; C4ZZ24; -.
DR SMR; C4ZZ24; -.
DR KEGG; ebw:BWG_3437; -.
DR HOGENOM; CLU_018678_1_0_6; -.
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..498
FT /note="ATPase RavA"
FT /id="PRO_1000215743"
SQ SEQUENCE 498 AA; 56389 MW; 3D2EDCAA17240BE9 CRC64;
MAHPHLLAER ISRLSSSLEK GLYERSHAIR LCLLAALSGE SVFLLGPPGI 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 GLPGEIKQQL EELESDWRKQ HALFSEQQKC LFIPGDWLGR
IEASLQDVGA QIRQAQQC