ID C5ADG3_BURGB Unreviewed; 773 AA.
AC C5ADG3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487};
DE AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE Short=ExoV subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
GN Name=recD {ECO:0000256|HAMAP-Rule:MF_01487};
GN OrderedLocusNames=bglu_1g10360 {ECO:0000313|EMBL:ACR28208.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR28208.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR28208.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR28208.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(2009).
CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC rapid and processive ATP-dependent bidirectional helicase activity.
CC Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC Chi site. The properties and activities of the enzyme are changed at
CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC and repair. Holoenzyme degrades any linearized DNA that is unable to
CC undergo homologous recombination. In the holoenzyme this subunit has
CC ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC assembled RecBC greatly stimulates nuclease activity and augments
CC holoenzyme processivity. Negatively regulates the RecA-loading ability
CC of RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01487};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP-
CC Rule:MF_01487}.
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DR EMBL; CP001503; ACR28208.1; -; Genomic_DNA.
DR RefSeq; WP_012735096.1; NC_012724.2.
DR AlphaFoldDB; C5ADG3; -.
DR STRING; 626418.bglu_1g10360; -.
DR KEGG; bgl:bglu_1g10360; -.
DR PATRIC; fig|626418.3.peg.3806; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_4; -.
DR Proteomes; UP000002187; Chromosome 1.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.10.1020; RecBCD complex, subunit RecD, N-terminal domain; 1.
DR HAMAP; MF_01487; RecD; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
DR InterPro; IPR041851; RecD_N_sf.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01487}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01487};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01487};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01487}; Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT DOMAIN 688..734
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT REGION 364..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 773 AA; 80478 MW; 3027DD76D4D8AD28 CRC64;
MKDLTEPFGF VGGLAERLPE PADFGLALAE GFARRIGMLS RRLGAPADAA RWAARAAFAA
SRATAAGHVC IALGALAARY AVSLDQVRAE LAASGVTAFG RAPRGADCPL VVDAQGRLYL
ARYFDYETRL ADALVAHARA ARPEADGALA PARLRESLAR YFAPPREGEI DWQRVAAVVA
LGGRLTIVSG GPGTGKTTTV VGVIACLIEL QPALRIALAA PTGKAAQRMQ EALHARAAGL
PAEFAAQLPR TSYTLHRLLG WLPGGRFRHH RDNPLPYDLV VVDEASMIDV ALAAHLLDAL
APGARLVLLG DKDQLAAVEA GAVFAELSAR PAFSAAGCER IAAALGVSPA AFVAALPDEA
RATAPAGATQ GANRAGADGR PASAAAPRRR GARPAPPEAG GMPVQRSLFD FDEVAASTDA
SACAAESASR AGQAGFADAP LEAWIEPDEL AWLDAWRIDE VQAARFDAGR TGMPAVPGPG
REPASHADAP AVGEPLADCV VWLERNYRFG LDSPIGRLSL AIRRGDAQAA LDALSTQADA
AARFIDDGGD ALAAATIERL ADGFAAYGRA LREVLAGGEP DPLPLFDVLN RFRVLCATRT
GARGADEINL RVAALVRRAV GVPLAVGAHW FAGRPVMVTR NDYALGLFNG DIGIALHDAQ
GALRVWFRGA DGLARAVSPA ALPPHDTAFA LTVHKSQGSE FDEAALVLPA AFGRVLSREL
VYTAITRARS RVQVIGPRAV LAQAIATRTQ RDSGLAARIA DAAQAAAEAE ARH
//
