RUVB_THEMA
ID RUVB_THEMA Reviewed; 334 AA.
AC Q56313;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
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=TM_1730;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8626340; DOI=10.1128/jb.178.9.2695-2700.1996;
RA Tong J., Wetmur J.G.;
RT "Cloning, sequencing, and expression of ruvB and characterization of RuvB
RT proteins from two distantly related thermophilic eubacteria.";
RL J. Bacteriol. 178:2695-2700(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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DR EMBL; U38840; AAB03727.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36795.1; -; Genomic_DNA.
DR PIR; A72217; A72217.
DR RefSeq; NP_229528.1; NC_000853.1.
DR RefSeq; WP_004082245.1; NZ_CP011107.1.
DR PDB; 1IN4; X-ray; 1.60 A; A=1-334.
DR PDB; 1IN5; X-ray; 2.00 A; A=1-334.
DR PDB; 1IN6; X-ray; 1.80 A; A=1-334.
DR PDB; 1IN7; X-ray; 1.90 A; A=1-334.
DR PDB; 1IN8; X-ray; 1.90 A; A=1-334.
DR PDB; 1J7K; X-ray; 1.80 A; A=1-334.
DR PDBsum; 1IN4; -.
DR PDBsum; 1IN5; -.
DR PDBsum; 1IN6; -.
DR PDBsum; 1IN7; -.
DR PDBsum; 1IN8; -.
DR PDBsum; 1J7K; -.
DR AlphaFoldDB; Q56313; -.
DR SMR; Q56313; -.
DR STRING; 243274.THEMA_05585; -.
DR DrugBank; DB02210; Hexane-1,6-Diol.
DR EnsemblBacteria; AAD36795; AAD36795; TM_1730.
DR KEGG; tma:TM1730; -.
DR eggNOG; COG2255; Bacteria.
DR InParanoid; Q56313; -.
DR OMA; IHRMSRP; -.
DR OrthoDB; 874197at2; -.
DR EvolutionaryTrace; Q56313; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..334
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000165617"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1IN4"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:1IN4"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1IN4"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:1IN4"
SQ SEQUENCE 334 AA; 37156 MW; 6F4BBFBFA7B9C7A9 CRC64;
MSEFLTPERT VYDSGVQFLR PKSLDEFIGQ ENVKKKLSLA LEAAKMRGEV LDHVLLAGPP
GLGKTTLAHI IASELQTNIH VTSGPVLVKQ GDMAAILTSL ERGDVLFIDE IHRLNKAVEE
LLYSAIEDFQ IDIMIGKGPS AKSIRIDIQP FTLVGATTRS GLLSSPLRSR FGIILELDFY
TVKELKEIIK RAASLMDVEI EDAAAEMIAK RSRGTPRIAI RLTKRVRDML TVVKADRINT
DIVLKTMEVL NIDDEGLDEF DRKILKTIIE IYRGGPVGLN ALAASLGVEA DTLSEVYEPY
LLQAGFLART PRGRIVTEKA YKHLKYEVPE NRLF
