ID   RUVB_TREPA              Reviewed;         350 AA.
AC   P96115; O83197;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN   Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; OrderedLocusNames=TP_0162;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
RX   PubMed=9332349; DOI=10.1016/s0378-1119(97)00234-5;
RA   Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y.,
RA   Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.;
RT   "Identification and transcriptional analysis of a Treponema pallidum operon
RT   encoding a putative ABC transport system, an iron-activated repressor
RT   protein homolog, and a glycolytic pathway enzyme homolog.";
RL   Gene 197:47-64(1997).
CC   -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC       cruciform structure in supercoiled DNA with palindromic sequence,
CC       indicating that it may promote strand exchange reactions in homologous
CC       recombination. RuvAB is a helicase that mediates the Holliday junction
CC       migration by localized denaturation and reannealing.
CC       {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00016};
CC   -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00016}.
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DR   EMBL; AE000520; AAC65150.1; -; Genomic_DNA.
DR   EMBL; U55214; AAC45724.1; -; Genomic_DNA.
DR   PIR; H71359; H71359.
DR   RefSeq; WP_010881609.1; NC_021490.2.
DR   AlphaFoldDB; P96115; -.
DR   SMR; P96115; -.
DR   IntAct; P96115; 5.
DR   STRING; 243276.TPANIC_0162; -.
DR   EnsemblBacteria; AAC65150; AAC65150; TP_0162.
DR   GeneID; 57878704; -.
DR   KEGG; tpa:TP_0162; -.
DR   eggNOG; COG2255; Bacteria.
DR   HOGENOM; CLU_055599_1_0_12; -.
DR   OMA; IHRMSRP; -.
DR   OrthoDB; 874197at2; -.
DR   Proteomes; UP000000811; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00016; DNA_helic_RuvB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041445; AAA_lid_4.
DR   InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008824; RuvB-like_N.
DR   InterPro; IPR008823; RuvB_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR42848; PTHR42848; 1.
DR   Pfam; PF17864; AAA_lid_4; 1.
DR   Pfam; PF05491; RuvB_C; 1.
DR   Pfam; PF05496; RuvB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00635; ruvB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; Helicase;
KW   Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN           1..350
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT                   /id="PRO_0000165623"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   CONFLICT        67
FT                   /note="L -> V (in Ref. 2; AAC45724)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  38665 MW;  69A2E3B3EB95CA1A CRC64;
     MDHTASLSPV RPEAQPTDDR ERALRPRLLK DFLGQEKTKR NLRLFIQAAR DRNESLDHLF
     LIGPPGLGKT TLAHITACEL GVECKVTGAP ALDKPKDLAG ILTALSERSV FFVDEIHRLK
     PAIEEMLYIA MEDYELDWVI GQGPSARTVR IPLPPFTLIG ATTRAGMVSS PLISRFGIVE
     RFEFYTPEEL AAIVQRSARL LDITLDARAA LALARCSRGT PRVANRLLRR IRDFAQVAGS
     AHISETIVRA GLAHLKIDEL GLELHDIQLL RVMIEHFGGG PVGAETLAIS LGESPETLED
     YYEPYLIQIG LMQRTPRGRM ATARAYAHLG LPVPEARTLT PHSPEQGTLL