RUVB_THET8
ID RUVB_THET8 Reviewed; 324 AA.
AC Q5SL87;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=TTHA0406;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=10485292; DOI=10.1007/s004380051049;
RA Yamada K., Fukuoh A., Iwasaki H., Shinagawa H.;
RT "Novel properties of the Thermus thermophilus RuvB protein, which promotes
RT branch migration of Holliday junctions.";
RL Mol. Gen. Genet. 261:1001-1011(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND SUBUNIT.
RX PubMed=11171970; DOI=10.1073/pnas.98.4.1442;
RA Yamada K., Kunishima N., Mayanagi K., Ohnishi T., Nishino T., Iwasaki H.,
RA Shinagawa H., Morikawa K.;
RT "Crystal structure of the Holliday junction migration motor protein RuvB
RT from Thermus thermophilus HB8.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1442-1447(2001).
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. RuvB is a Mg(2+)-
CC dependent, DNA-dependent ATPase with an equal preference for
CC supercoiled and linear duplex DNA. It can promote Holliday junction
CC migration alone. {ECO:0000255|HAMAP-Rule:MF_00016,
CC ECO:0000269|PubMed:10485292}.
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 ECO:0000269|PubMed:10485292};
CC -!- ACTIVITY REGULATION: The activity of RuvB is enhanced by RuvA.
CC {ECO:0000269|PubMed:10485292}.
CC -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016,
CC ECO:0000269|PubMed:10485292, ECO:0000269|PubMed:11171970}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC Rule:MF_00016}.
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DR EMBL; AB015236; BAA76480.2; -; Genomic_DNA.
DR EMBL; AP008226; BAD70229.1; -; Genomic_DNA.
DR RefSeq; WP_011227913.1; NC_006461.1.
DR RefSeq; YP_143672.1; NC_006461.1.
DR PDB; 1HQC; X-ray; 3.20 A; A/B=1-324.
DR PDB; 1IXR; X-ray; 3.30 A; C=1-312.
DR PDB; 1IXS; X-ray; 3.20 A; B=1-318.
DR PDBsum; 1HQC; -.
DR PDBsum; 1IXR; -.
DR PDBsum; 1IXS; -.
DR AlphaFoldDB; Q5SL87; -.
DR SMR; Q5SL87; -.
DR IntAct; Q5SL87; 1.
DR STRING; 300852.55771788; -.
DR DrugBank; DB00173; Adenine.
DR PRIDE; Q5SL87; -.
DR EnsemblBacteria; BAD70229; BAD70229; BAD70229.
DR GeneID; 3168960; -.
DR KEGG; ttj:TTHA0406; -.
DR PATRIC; fig|300852.9.peg.406; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_0; -.
DR OMA; IHRMSRP; -.
DR PhylomeDB; Q5SL87; -.
DR EvolutionaryTrace; Q5SL87; -.
DR Proteomes; UP000000532; 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..324
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000165619"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1IXR"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1HQC"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1IXR"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:1HQC"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1HQC"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:1HQC"
SQ SEQUENCE 324 AA; 35974 MW; F23C50F71F14D7DB CRC64;
MEDLALRPKT LDEYIGQERL KQKLRVYLEA AKARKEPLEH LLLFGPPGLG KTTLAHVIAH
ELGVNLRVTS GPAIEKPGDL AAILANSLEE GDILFIDEIH RLSRQAEEHL YPAMEDFVMD
IVIGQGPAAR TIRLELPRFT LIGATTRPGL ITAPLLSRFG IVEHLEYYTP EELAQGVMRD
ARLLGVRITE EAALEIGRRS RGTMRVAKRL FRRVRDFAQV AGEEVITRER ALEALAALGL
DELGLEKRDR EILEVLILRF GGGPVGLATL ATALSEDPGT LEEVHEPYLI RQGLLKRTPR
GRVATELAYR HLGYPPPVGP LLEP
