ID A0A097R8A5_HAFAL Unreviewed; 618 AA.
AC A0A097R8A5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:AIU74952.1};
GN ORFNames=AT03_17595 {ECO:0000313|EMBL:AIU74952.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU74952.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU74952.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU74952.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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; CP009706; AIU74952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A097R8A5; -.
DR KEGG; hav:AT03_17595; -.
DR PATRIC; fig|1453496.5.peg.3614; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_6; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000029986; Chromosome.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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:AIU74952.1};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487, ECO:0000313|EMBL:AIU74952.1};
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:UP000029986}.
FT DOMAIN 170..365
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 618 AA; 67781 MW; EAD4F22474DF4078 CRC64;
MIFDLLLNMG AQKYLRSLDV QFARLMANQG QPHLALAAAL VSLETASGHV CLPLSQLSLT
SLNKQFPDFA NELSQLIGDM DEAAWQACLL AEAEVSDGSY PAPLVLQNQR LYLQRLWQDE
GVVATFFAGN EAVSDESAPA LSAILSQLFP ARSEDAEVNW QQVAAAVAAT RQVSVISGGP
GTGKTTTVAR LLTALVRLHP QRKLRIQLAA PTGKAAARLT ESLGKAVEAL GLTPAEHEVI
PQEAYTLHRL LGAQPNSIRL RYHRENPLHV DVLVVDEASM VDLPMMSKLI AALPQRARLI
LLGDRDQLAS VEAGAVLGDL CRFSEFGYRP ERAKQLSVLC QTAIPAGAEQ PDIAVRDSIC
LLRKSYRFDA NSGIGQLASA VNGGDVVAAR RCFDGKFSDI SWSPMTKDED YSTLIQTCVE
GYRSTLQRVR EQADAAEVLE SFSRFRLLCA LREGPFGQSG LNDRIELALA KARLIHKPMQ
AHQRWYSGRP VMVTRNDSSL GLFNGDIGIA LADAENNIRV YFQLPDGSIK SVQPSRLPQT
ETAYAMTVHK SQGSEFEHTL LVLPADFSPI VTRELLYTAI TRAKNQLTLF SREQILKTAI
RTPTLRRSGL MERMMLPV
//
