ID   RAVA_PHOLL              Reviewed;         503 AA.
AC   Q7NA81;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=plu0054;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571859; CAE12349.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7NA81; -.
DR   SMR; Q7NA81; -.
DR   STRING; 243265.plu0054; -.
DR   PRIDE; Q7NA81; -.
DR   EnsemblBacteria; CAE12349; CAE12349; plu0054.
DR   KEGG; plu:plu0054; -.
DR   eggNOG; COG0714; Bacteria.
DR   HOGENOM; CLU_018678_1_0_6; -.
DR   OMA; HANAFEY; -.
DR   Proteomes; UP000002514; 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..503
FT                   /note="ATPase RavA"
FT                   /id="PRO_0000209373"
SQ   SEQUENCE   503 AA;  59052 MW;  C02C152C374F5091 CRC64;
     MVRIMLLAEK IVCLSHYLES GLYERQQTIR LCLLAALCGE SVFLLGPPGI AKSLIARRLK
     FAFRDARAFE YLMTRFSTPE EIFGPLSIQA LKEEGRYQRL TNGYLPETEI VFLDEIWKAG
     PAILNTLLTA INERKFRNGD TEDKIPMRLL ITASNELPEA DNSLEALYDR MLIRIWLDKI
     QEKKNFRALL SSHKNENDNP VPANIQITSE EFHQWQKEID KIVLPDSCFD IIYHLRQQLD
     ATEHSPYVSD RRWKKAIHLL QASAFFNGRK EISPLDLILL KDCLWHDLHS FKLLPQYLNT
     LMTEQAYRQR ILSQQIDSLY HQWTQACQDK NDQQALKLEK QTRLFGRKIQ YSLPDHINEE
     KLILFLHTPL HLHDIKVNFI ELEKKALNIW INKGRELSAR LNGIGFPQNI AAEVNSAHQP
     EIFDISRRSS TLYLPDHQHQ QNEENNEWQE RLEKFNQEIH HQHQLFNQHQ PCLFIESHWL
     ATIEQSFIQL SDKIKQLKIK IGS