ID   RECD_MYCS2              Reviewed;         554 AA.
AC   A0QS28;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=RecBCD enzyme subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE            EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01487};
DE   AltName: Full=Exonuclease V subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE            Short=ExoV subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
GN   Name=recD {ECO:0000255|HAMAP-Rule:MF_01487};
GN   OrderedLocusNames=MSMEG_1325, MSMEI_1288;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17496093; DOI=10.1128/jb.00332-07;
RA   Stephanou N.C., Gao F., Bongiorno P., Ehrt S., Schnappinger D., Shuman S.,
RA   Glickman M.S.;
RT   "Mycobacterial nonhomologous end joining mediates mutagenic repair of
RT   chromosomal double-strand DNA breaks.";
RL   J. Bacteriol. 189:5237-5246(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18281464; DOI=10.1101/gad.1631908;
RA   Aniukwu J., Glickman M.S., Shuman S.;
RT   "The pathways and outcomes of mycobacterial NHEJ depend on the structure of
RT   the broken DNA ends.";
RL   Genes Dev. 22:512-527(2008).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=21219454; DOI=10.1111/j.1365-2958.2010.07463.x;
RA   Gupta R., Barkan D., Redelman-Sidi G., Shuman S., Glickman M.S.;
RT   "Mycobacteria exploit three genetically distinct DNA double-strand break
RT   repair pathways.";
RL   Mol. Microbiol. 79:316-330(2011).
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       Holoenzyme degrades any linearized DNA that is unable to undergo
CC       homologous recombination. In the holoenzyme this subunit has ssDNA-
CC       dependent ATPase and 5'-3' helicase activity. When added to pre-
CC       assembled RecBC greatly stimulates nuclease activity and augments
CC       holoenzyme processivity (By similarity). Unlike the case in E.coli,
CC       suppresses RecA-dependent homologous recombination, is instead required
CC       for single-strand annealing pathway repair of DSB. {ECO:0000250,
CC       ECO:0000269|PubMed:21219454}.
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:0000255|HAMAP-
CC         Rule:MF_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01487}.
CC   -!- DISRUPTION PHENOTYPE: Unlike E.coli, triple recB-recC-recD deletion is
CC       no more sensitive to DNA damaging agents (UV light sensitivity,
CC       mitomycin C, methyl methanesulphonate or ionizing radiation) than wild-
CC       type; has reduced resistance to H(2)O(2) which is exacerbated by
CC       further adnA-adnB deletion. Triple mutants have no effect on homologous
CC       recombination or on NHEJ of blunt-end, 5'- or 3'-overhang DSBs or on
CC       incompatible 3'-chromosomal overhangs. However the triple mutant
CC       disrupts all single-strand annealing repair of DSB.
CC       {ECO:0000269|PubMed:17496093, ECO:0000269|PubMed:18281464,
CC       ECO:0000269|PubMed:21219454}.
CC   -!- SIMILARITY: Belongs to the RecD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01487}.
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DR   EMBL; CP000480; ABK75071.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37764.1; -; Genomic_DNA.
DR   RefSeq; WP_011727604.1; NZ_SIJM01000030.1.
DR   RefSeq; YP_885716.1; NC_008596.1.
DR   AlphaFoldDB; A0QS28; -.
DR   SMR; A0QS28; -.
DR   STRING; 246196.MSMEI_1288; -.
DR   EnsemblBacteria; ABK75071; ABK75071; MSMEG_1325.
DR   EnsemblBacteria; AFP37764; AFP37764; MSMEI_1288.
DR   GeneID; 66732786; -.
DR   KEGG; msg:MSMEI_1288; -.
DR   KEGG; msm:MSMEG_1325; -.
DR   PATRIC; fig|246196.19.peg.1313; -.
DR   eggNOG; COG0507; Bacteria.
DR   OMA; MIDLEMM; -.
DR   OrthoDB; 961809at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   Gene3D; 1.10.10.1020; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
DR   InterPro; IPR041851; RecD_N.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01447; recD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..554
FT                   /note="RecBCD enzyme subunit RecD"
FT                   /id="PRO_0000425943"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   554 AA;  59516 MW;  3947B550498BD62C CRC64;
     MSLLEAFAEI LEPADVHVAQ RLTVLADEPD ASVELAVALA VRALRGGSVC VDLRSVAGQV
     ELPDLPWPDP DAWLAALAAS PLLGQPPVLR LFGDLLYLDR YWLEEQQVCD DVLALVSARP
     GGAVPDVSRL FGAGFEEQRA AAKVALSQGL TVLTGGPGTG KTTTVARLLA LLAEQAALAG
     KPSPRIALAA PTGKAAARLQ EAVQLEIDQL DLIERRRLTG LHATTLHRLL GPRPDTSSRF
     RHHRANRLPH DVIVVDETSM VSLTMMARLL EAVRPQTRLV LVGDPDQLAS VEAGAVLADL
     VEGLGSRGVA ELKTSHRFGE SIGALASAIR TGDADAALAV LAAGGEHIEW VHEDPVEQLR
     EVVVPHAMRL RQAAILGDQR EALATLDEHR LLCAHRRGPA GVDHWNRQVQ RWLGEETGEP
     LWGSWYVGRP ILVTANDYGL KLYNGDTGVV VATPDGMRAV IGDAGTFATG RLTDVETMHA
     MTIHKSQGSQ ADEVTVLLPS EDSRLLTREL FYTAVTRAKT RVRVVGAEAE VRAAIERQAV
     RATGLRKRLR PAGV