ID A0A0B4XNI2_9GAMM Unreviewed; 597 AA.
AC A0A0B4XNI2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:AJD49929.1};
GN ORFNames=S7S_17585 {ECO:0000313|EMBL:AJD49929.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD49929.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD49929.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD49929.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004387; AJD49929.1; -; Genomic_DNA.
DR RefSeq; WP_008734788.1; NZ_CP004387.1.
DR AlphaFoldDB; A0A0B4XNI2; -.
DR STRING; 391936.S7S_17585; -.
DR KEGG; apac:S7S_17585; -.
DR HOGENOM; CLU_007524_1_2_6; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000006764; 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: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 Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AJD49929.1};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AJD49929.1};
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:UP000006764}.
FT DOMAIN 15..61
FT /note="RecBCD enzyme subunit RecD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21185"
FT DOMAIN 525..571
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 597 AA; 64532 MW; 5A3EC72C59298B63 CRC64;
MSAALQWLEA RVGRGGLRPL DVSLARFVAE HGGDDHAVWL TALVSFMSTQ GHVCLDLAHA
PAEPFDLPDC PWRPDTPPPI DGTLIGAPGD NAPLILDDTR LYLSRHYQAE GRVAAAVRHR
LMLRELPTGL TGQLAGTLFP DNAEETDWQR IAAINCTLHR FGIITGGPGT GKTWTVTRML
ALQLLVAHTL APDDPLPRIR LAAPTGKAAA RLTESLRAAL PSLQIDDALR DALPSEAVTL
HRLLGAGRDG RPRYTASRPL PVDIVVVDEA SMIDLGLMTQ LVAALPEQAS LYLVGDRDQL
ASVEAGSVFA DLCGQGGTQF SAPLAERLAL EGIHVPDSAQ QTSLVDDTVV RLTRTHRFGH
TSGIAQLAEA VRTGDVRAVQ ALRDTPPPDL AWAAPDRAAL IQYAVNALKP MLTLAATGAP
AEDVLTAFGR FRILCALRRG PWGVEQINTQ ITRALRRAGL TDSEEWYPGR AVLLTRNDWA
LGLFNGDAGV AVLDPEDGQL KVAFLAPDEQ VRYVPPVRLP AFEECWAMTI HKSQGSEFDE
VVLVLPESDS LILGRELVYT GITRAKERVM MTMDERSLNA AMSRSVSRHT GLGDQII
//
