ID A0A143G6Y8_9GAMM Unreviewed; 593 AA.
AC A0A143G6Y8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=AMD27_14495 {ECO:0000313|EMBL:AMW79990.1};
OS Acinetobacter sp. TGL-Y2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW79990.1, ECO:0000313|Proteomes:UP000076238};
RN [1] {ECO:0000313|Proteomes:UP000076238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA Zhang G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015110; AMW79990.1; -; Genomic_DNA.
DR RefSeq; WP_067661808.1; NZ_CP015110.1.
DR AlphaFoldDB; A0A143G6Y8; -.
DR STRING; 1407071.AMD27_14495; -.
DR KEGG; acv:AMD27_14495; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000076238; 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; 2.
DR HAMAP; MF_01487; RecD; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01447; recD; 1.
DR PANTHER; PTHR43788:SF6; DNA HELICASE B; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW 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|HAMAP-Rule:MF_01487};
KW Reference proteome {ECO:0000313|Proteomes:UP000076238}.
FT DOMAIN 514..558
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 147..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 593 AA; 66587 MW; 54AAC788B34A8C49 CRC64;
MENKQQRESQ APQWVRTWAE FILKQASNDI KQNEQSINLI EQILLATTQG DSCIEKPESA
LEQLHHLMVT DEQASHQQVA PFVSDEQYLY LYRYWSLEQR LALQVKRLKQ QNIDPVDVQA
FEHLLQDVHQ KSALSMVAKN ALNIITGGPG TGKTYTLARI IAVLSQAMPD IRIAMAAPTG
KAAQRMKEAM QSSFADEKLN ALGLVSARLK QQDTFTLHRL LGLGTQFKAR FNLKQPLPYD
VIVIDEASML DLNLATLLFE AVPDHCRLIL LGDANQLASV DVGSVLADLQ NVDALAENCV
NLITTRRFKA GARIGETAQF IQSAKYQTDS AQMLHAFEKQ IVTAGELQPI PLKQGMNDVV
QLEYITDQST DQISAVALTQ YYEKLSSGYQ DYFHALDAYM QNGYTEENVP KVIDAFDRYR
ILTAIRYGEL GLDRLNGEMQ KALLKALPRI VKQGDWYIGR PVMMSYNDYQ LGVSNGDIGL
CFKHRTQADL FEVYFPSLDK WLPATRLPKS IQTAFALTIH KSQGSEFMHT TVVLDESATK
LLSQELIYTA ITRAKSVVSL LVSPNALRQA LTIKTTRRSG LVNKMNKIVL SNI
//