AC MF_01485; DC Protein; auto TR HAMAP; MF_01485; -; 1; level=0 XX Names: RecB XX ID RECB DE RecName: Full=RecBCD enzyme subunit RecB; DE EC=3.1.11.5; DE AltName: Full=Exonuclease V subunit RecB; DE Short=ExoV subunit RecB; DE AltName: Full=Helicase/nuclease RecBCD subunit RecB; GN Name=recB; XX 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 CC contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA CC onto ssDNA. 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; case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; end case CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute CC to DNA-binding. Interacts with RecA. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase CC and has ATP-dependent 3'-5' helicase function. This domain interacts CC with RecC. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with CC RecD. It interacts with RecA, facilitating its loading onto ssDNA. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. XX DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1; trigger=yes DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1; trigger=yes DR Pfam; PF00580; UvrD-helicase; 1; trigger=no DR Pfam; PF13361; UvrD_C; 1; trigger=no DR TIGRFAMs; TIGR00609; recB; 1; trigger=no XX KW ATP-binding KW DNA damage KW DNA repair KW DNA-binding KW Exonuclease KW Helicase KW Hydrolase case KW Magnesium KW Metal-binding end case KW Nuclease KW Nucleotide-binding XX case GO GO:0000287; F:magnesium ion binding end case GO GO:0003678; F:DNA helicase activity GO GO:0005524; F:ATP binding GO GO:0003677; F:DNA binding GO GO:0000724; P:double-strand break repair via homologous recombination XX FT From: RECB_ECOLI (P08394) FT REGION Nter..850 FT /note="DNA-binding and helicase activity, interacts with FT RecC" FT REGION 900..Cter FT /note="Nuclease activity, interacts with RecD and RecA" FT ACT_SITE 1080 FT /note="For nuclease activity" FT Group: 1; Condition: D FT METAL 956 FT /note="Magnesium; via tele nitrogen" FT Group: 1; Condition: H FT METAL 1067 FT /note="Magnesium" FT Group: 1; Condition: D FT METAL 1080 FT /note="Magnesium" FT Group: 1; Condition: D XX Size: 987-1496; Related: None; Template: P08394; Scope: Bacteria; Actinobacteria Bacteria; Bacteroidetes Bacteria; Chlorobi Bacteria; Deferribacteres Bacteria; Proteobacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: in PARRH, GORPV, LEPBA, LEPBP, SHEB5 Comments: None XX # Revision 1.11 2019/11/19 //