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Database: UniProt
Entry: A0A143G6Y8_9GAMM
LinkDB: A0A143G6Y8_9GAMM
Original site: A0A143G6Y8_9GAMM 
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
//
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