RUVB_CORGL
ID RUVB_CORGL Reviewed; 360 AA.
AC Q9AE09;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 135.
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};
GN OrderedLocusNames=Cgl1660, cg1869;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RA Berens S., Kalinowski J., Puehler A.;
RT "The role of Corynebacterium glutamicum secretion genes secD, secF and secG
RT in transporting the Streptomyces griseus alpha-amylase.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK19840.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAF20042.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF038651; AAK19840.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000036; BAB99053.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20042.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_600872.1; NC_003450.3.
DR AlphaFoldDB; Q9AE09; -.
DR SMR; Q9AE09; -.
DR STRING; 196627.cg1869; -.
DR KEGG; cgb:cg1869; -.
DR KEGG; cgl:Cgl1660; -.
DR PATRIC; fig|196627.13.peg.1620; -.
DR eggNOG; COG2255; Bacteria.
DR HOGENOM; CLU_055599_1_0_11; -.
DR OMA; IHRMSRP; -.
DR Proteomes; UP000000582; 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; EXP:CollecTF.
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..360
FT /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT /id="PRO_0000165524"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT CONFLICT 12..22
FT /note="IPPRRNGGQGR -> FHLVETVVKAV (in Ref. 1; AAK19840)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="I -> D (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38603 MW; 7554F0BF3BFDF954 CRC64;
MERTEFEIPG GIPPRRNGGQ GRAADTNVDA NLKPDEYDAE VTLRPKSLTE FIGQPKVRDQ
LSLVLTGAKN RGVVPDHVLL SGPPGLGKTT MAMIIAQELG TSLRMTSGPA LERAGDLAAM
LSNLMEGDVL FIDEIHRIAR PAEEMLYMAM EDFRIDVIVG KGPGATSIPL EIPPFTLVGA
TTRSGMLTGP LRDRFGFTAQ MEFYDVPDLT KVVKRTAKIL DVGIDNDAAV EIASRSRGTP
RIANRLLRRV RDFAEVHADG HITMGAANAA LIVFDVDEVG LDRLDRAVLD ALIRGHGGGP
VGVNTLAVAV GEEPGTVEEV CEPYLVRAGM IARTGRGRVA TAAAWRHLGL EPPEGTIGDY
