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Database: UniProt
Entry: A0QS29
LinkDB: A0QS29
Original site: A0QS29 
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   05-DEC-2018, entry version 91.
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   Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
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
RT   orthology 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.,
RA   Shuman S., 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
RT   structure of 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
RT   break 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
CC       highly rapid and processive ATP-dependent bidirectional helicase
CC       activity. Holoenzyme degrades any linearized DNA that is unable to
CC       undergo homologous recombination. In the holoenzyme this subunit
CC       contributes DNA-dependent ATPase activity, exonuclease activity
CC       and 3'-5' helicase activity (By similarity). Unlike the case in
CC       E.coli, suppresses RecA-dependent homologous recombination, is
CC       instead required for single-strand annealing pathway repair of
CC       DSB. {ECO:0000250, ECO:0000269|PubMed:21219454}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in
CC         either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5;
CC         Evidence={ECO:0000255|HAMAP-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
CC       contribute to DNA-binding. Interacts with RecA.
CC       {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent
CC       ATPase and has ATP-dependent 3'-5' helicase function. This domain
CC       interacts with RecC. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The C-terminal domain has nuclease activity and interacts
CC       with RecD. It interacts with RecA, facilitating its loading onto
CC       ssDNA. {ECO:0000255|HAMAP-Rule:MF_01485}.
CC   -!- DISRUPTION PHENOTYPE: Unlike E.coli, triple recB-recC-recD
CC       deletion is no more sensitive to DNA damaging agents (UV light
CC       sensitivity, mitomycin C, methyl methanesulphonate or ionizing
CC       radiation) than wild-type; has reduced resistance to H(2)O(2)
CC       which is exacerbated by further adnA-adnB deletion. Triple mutants
CC       have no effect on homologous recombination or on NHEJ of blunt-
CC       end, 5'- or 3'-overhang DSBs or on incompatible 3'-chromosomal
CC       overhangs. However the triple mutant disrupts all single-strand
CC       annealing repair of DSB. {ECO:0000269|PubMed:17496093,
CC       ECO:0000269|PubMed:18281464, ECO:0000269|PubMed:21219454}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01485}.
DR   EMBL; CP000480; ABK70050.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37765.1; -; Genomic_DNA.
DR   RefSeq; WP_011727605.1; NZ_CP009494.1.
DR   RefSeq; YP_885717.1; NC_008596.1.
DR   ProteinModelPortal; A0QS29; -.
DR   SMR; A0QS29; -.
DR   STRING; 246196.MSMEG_1327; -.
DR   EnsemblBacteria; ABK70050; ABK70050; MSMEG_1327.
DR   EnsemblBacteria; AFP37765; AFP37765; MSMEI_1289.
DR   GeneID; 4532889; -.
DR   KEGG; msb:LJ00_06615; -.
DR   KEGG; msg:MSMEI_1289; -.
DR   KEGG; msm:MSMEG_1327; -.
DR   PATRIC; fig|246196.19.peg.1314; -.
DR   eggNOG; ENOG4107QKA; Bacteria.
DR   eggNOG; COG1074; LUCA.
DR   HOGENOM; HOG000258330; -.
DR   KO; K03582; -.
DR   OMA; VICPYLW; -.
DR   OrthoDB; POG091H02P3; -.
DR   BioCyc; MSME246196:G1H7P-1338-MONOMER; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; 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; 3.90.320.10; -; 1.
DR   HAMAP; MF_01485; RecB; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
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   InterPro; IPR034739; UvrD/AddA_N.
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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Exonuclease; Helicase; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1   1083       RecBCD enzyme subunit RecB.
FT                                /FTId=PRO_0000425941.
FT   DOMAIN        1    323       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   DOMAIN      349    607       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   NP_BIND      21     28       ATP. {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   REGION        1    745       DNA-binding and helicase activity,
FT                                interacts with RecC. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   REGION      765   1083       Nuclease activity, interacts with RecD
FT                                and RecA. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   ACT_SITE    975    975       For nuclease activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL       830    830       Magnesium; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL       962    962       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   METAL       975    975       Magnesium. {ECO:0000255|HAMAP-
FT                                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
//
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