RUVB_MYCSK
ID RUVB_MYCSK Reviewed; 357 AA.
AC A1UFA4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Mkms_2314;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL91512.1; -; Genomic_DNA.
DR RefSeq; WP_011559665.1; NC_008705.1.
DR AlphaFoldDB; A1UFA4; -.
DR SMR; A1UFA4; -.
DR STRING; 189918.Mkms_2314; -.
DR EnsemblBacteria; ABL91512; ABL91512; Mkms_2314.
DR KEGG; mkm:Mkms_2314; -.
DR HOGENOM; CLU_055599_1_0_11; -.
DR OMA; IHRMSRP; -.
DR OrthoDB; 874197at2; -.
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; SOS response.
FT CHAIN 1..357
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000322817"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
SQ SEQUENCE 357 AA; 37803 MW; AFFBAD40D0100A3F CRC64;
MGRFDDAGAQ DAEPDDRDVS PALTVGEGDI DASLRPRSLG EFIGQPRVRE QLQLVLEGAK
NRGGTPDHIL LSGPPGLGKT SLAMIIAAEL SSSLRVTSGP ALERAGDLAA MLSNLVEGDV
LFIDEIHRIA RPAEEMLYLA MEDFRVDVVV GKGPGATSIP LEVAPFTLVG ATTRSGALTG
PLRDRFGFTA HMDFYEPAEL ERVLARSAGI LGIHLGTEAG AEIARRSRGT PRIANRLLRR
VRDYAEVRAD GVITRDIAKA ALEVYDVDEL GLDRLDRAVL SALIRSFGGG PVGVSTLAVA
VGEEPTTVEE VCEPFLVRAG MIARTPRGRV ATASAWTHLG LTPPSGITGL GQTGLFD