ID Q88DZ6_PSEPK Unreviewed; 691 AA.
AC Q88DZ6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
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 ECO:0000313|EMBL:AAN70245.1};
GN OrderedLocusNames=PP_4672 {ECO:0000313|EMBL:AAN70245.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN70245.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN70245.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70245.1; -; Genomic_DNA.
DR RefSeq; NP_746781.1; NC_002947.4.
DR RefSeq; WP_010955327.1; NC_002947.4.
DR AlphaFoldDB; Q88DZ6; -.
DR STRING; 160488.PP_4672; -.
DR PaxDb; 160488-PP_4672; -.
DR GeneID; 83682380; -.
DR KEGG; ppu:PP_4672; -.
DR PATRIC; fig|160488.4.peg.4980; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_6; -.
DR OrthoDB; 9803432at2; -.
DR PhylomeDB; Q88DZ6; -.
DR BioCyc; PPUT160488:G1G01-4985-MONOMER; -.
DR Proteomes; UP000000556; Chromosome.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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; IPR049550; RecD_N.
DR InterPro; IPR041851; RecD_N_sf.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01447; recD; 1.
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; PF21185; RecD_N; 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 Endonuclease {ECO:0000313|EMBL:AAN70245.1};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AAN70245.1};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AAN70245.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AAN70245.1};
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:UP000000556}.
FT DOMAIN 37..155
FT /note="RecBCD enzyme subunit RecD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21185"
FT DOMAIN 618..660
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 691 AA; 75545 MW; 2215BA660F40E66B CRC64;
MSRSLVDLLP TPLHAEHLLA LAPQHNSADL LQLLDRWVER GWLRALDRAF VSFLEERAPG
SDPLLLLAAA LASHQLGHGH VCLDLQQTLA EPDFALSLPP EGDALIGPLL LPSQLLANLD
LNAWLQRISA SPLVAAGDTP GQQARPLVRS GERLYLRRYW SYERRIDQAL RQRLSQAEAP
PADLPERLAQ LFEGGAPAGQ VDWQKLACAL ATRAGFSIIT GGPGTGKTTT VVRLLALLQA
PAVEQGRPLR IRLAAPTGKA AARLTESIGQ QVERLQVSAE VRGQIPTEVS TVHRLLGSRP
GSRHFRHHAG NPLPLDVLVV DEASMIDLEM MANLLDALPP RARLVLLGDK DQLASVEAGA
VLGDLCRDAE EGFYSPATAA WLQQVSGESL AGSGLKAGDE QRHPLAQQVV MLRFSRRFGE
GSGIGQLARL VNRQDAHAAR NLLAAPPADV HSLSLKHEQD RAFDRLLLDG LNRGTDGPQG
YRSYLRTLGR YRPALDTAFD DPAWEQWAGK VLRSFEDFQL LCAVRRGAWG VEGLNERVAR
VLHNAGLIDS QQPWYEGRPV LVTRNDYGLG LMNGDIGIAL RLPDEHGQPL LRVAFPRNDG
SGGVRFVLPS RLNEVETVFA MTVHKSQGSE FSHTALVLPE ALNPVLTKEL VYTGITRAKH
CFSLVEPRQG IFEEAVARKV RRISGLMLEQ V
//
