RECB_MYCS2
ID RECB_MYCS2 Reviewed; 1083 AA.
AC A0QS29;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000255|HAMAP-Rule:MF_01485};
GN OrderedLocusNames=MSMEG_1327, MSMEI_1289;
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 contributes
CC DNA-dependent ATPase activity, exonuclease activity and 3'-5' helicase
CC activity (By similarity). Unlike the case in E.coli, suppresses RecA-
CC dependent homologous recombination, is instead required for single-
CC 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_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000255|HAMAP-Rule:MF_01485}.
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. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
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 helicase family. UvrD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01485}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK70050.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37765.1; -; Genomic_DNA.
DR RefSeq; WP_011727605.1; NZ_SIJM01000030.1.
DR RefSeq; YP_885717.1; NC_008596.1.
DR AlphaFoldDB; A0QS29; -.
DR SMR; A0QS29; -.
DR STRING; 246196.MSMEI_1289; -.
DR EnsemblBacteria; ABK70050; ABK70050; MSMEG_1327.
DR EnsemblBacteria; AFP37765; AFP37765; MSMEI_1289.
DR GeneID; 66732787; -.
DR KEGG; msg:MSMEI_1289; -.
DR KEGG; msm:MSMEG_1327; -.
DR PATRIC; fig|246196.19.peg.1314; -.
DR eggNOG; COG1074; Bacteria.
DR OMA; VDYKTNW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01485; RecB; 1.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 2.
DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 2.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00609; recB; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1083
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000425941"
FT DOMAIN 1..323
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 349..607
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..745
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 765..1083
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 975
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 830
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 962
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 975
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1083 AA; 117443 MW; A531F5FBA85EB748 CRC64;
MKVFDLLGPL PAPNTTTVLE ASAGTGKTFA LAGLVTRFVA EGVATLDQML LITFGRAASQ
ELRERVRAQI VAALVALDDP SRACNDLEEY LVKTDQQARR RRLRDALAGF DAATIATTHQ
FCQIVLKSLG VAGDSDAGVT LVESLDDLVS EIVDDLYLAH FGGQKDDPEL SYPEALKLAR
VVVGNPATQL RPRDPDPDSP AAVRLKFARD VLAELEIRKR RRGVLGYDDL LTRLADALEP
EDSPARVRMQ QRWPIVMVDE FQDTDPVQWQ VIERAFSGRS TLVLIGDPKQ AIYAFRGGDI
ATYLRAAATA GDKQTLGTNW RSDRALVDRL QAVLRGAQLG GPDIVVHDVQ ARHQGHRLVG
APRNDPFRLR VVSRKPGNTR VIPIDQLRRH IGRDLAADIS ALLNSGATWC DQPVQAKDIA
VITETHKDAR ACHAALLAAG IPAVYTGDSD VFTSEAAEDW LYLLEAFDQP HRPGLVRAAA
ATMFFGETAE SLAAGGDALT DRVADTLREW AGHARERGVA AIFEAAQLAG MGKRVLSWQG
GERLMTDLAH MTQLLQDTAH REGFGLAALR DWLRTQRSER GGESERNRRL DSDAAAVQIM
TVWVSKGLQF PVVYLPFAFN RYVPEPDLVL FHDDGQRCLH VGGADPAVAR AGRAEAAGDD
SRLTYVALTR AQSQVVAWWA PSYDEPNGGL SRLMRGRAPG EAIVPDKCSP PKISDEDALE
RLRAWEAAGG PVIEESVIGA VSPVPPEPAP EDLAARKFFR AIDMAWKRTS YSGLLRAAET
AGVGVSSEPE VTERDDEFDD IPVVAPAEGA DVPSPMAHLP TGAAFGSLVH AVLETADPFA
EDLTAELATH IDAHSQHWPV EVETAELAAA LVPMHDTPLG PLAPGLTLRQ IGLRDRLCEL
DFEFPMAGGD LRGGRFARLS DVGELLREYL PADDPLAVYA ERLSTGILGV QPLRGYLSGS
VDAVLRVGEK FVIVDYKTNW LGTGDGTLTA ADYGRRRMVE AMLHSDYPLQ ALLYAVVLHR
YLGWRLSGYD PATHLGGVLY LFVRGMCGAG TPVVDGHPAG VFSWEPPADL VVALSKLLDA
EAP
