RECC_MYCS2
ID RECC_MYCS2 Reviewed; 1085 AA.
AC A0QS30; I7G3M1;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=RecBCD enzyme subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01486};
DE AltName: Full=Exonuclease V subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
DE Short=ExoV subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486};
GN Name=recC {ECO:0000255|HAMAP-Rule:MF_01486}; OrderedLocusNames=MSMEG_1328;
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 recognizes the
CC wild-type Chi sequence, and when added to isolated RecB increases its
CC ATP-dependent helicase processivity (By similarity). Unlike the case in
CC E.coli, suppresses RecA-dependent homologous recombination, is instead
CC required for single-strand annealing pathway repair of DSB.
CC {ECO:0000250, 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_01486};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01486}.
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 RecC family. {ECO:0000255|HAMAP-
CC Rule:MF_01486}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK73955.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK73955.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP37766.1; -; Genomic_DNA.
DR RefSeq; WP_014877040.1; NZ_SIJM01000030.1.
DR RefSeq; YP_885718.1; NC_008596.1.
DR AlphaFoldDB; A0QS30; -.
DR SMR; A0QS30; -.
DR STRING; 246196.MSMEI_1290; -.
DR EnsemblBacteria; ABK73955; ABK73955; MSMEG_1328.
DR EnsemblBacteria; AFP37766; AFP37766; MSMEI_1290.
DR GeneID; 66732788; -.
DR KEGG; msg:MSMEI_1290; -.
DR KEGG; msm:MSMEG_1328; -.
DR PATRIC; fig|246196.19.peg.1315; -.
DR eggNOG; COG1330; Bacteria.
DR OrthoDB; 1320159at2; -.
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; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01486; RecC; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006697; RecC.
DR InterPro; IPR041500; RecC_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR Pfam; PF17946; RecC_C; 1.
DR PIRSF; PIRSF000980; RecC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR01450; recC; 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..1085
FT /note="RecBCD enzyme subunit RecC"
FT /id="PRO_0000425942"
SQ SEQUENCE 1085 AA; 120353 MW; F4D9A81AA6A277C4 CRC64;
MALHLHRAER TDLLADGLAA LLSDPLPDPF ATELVLVPAK GVERWLSQRL SNRLGVCAAV
EFRNPRSLIA ELTGTADDDP WSPDAMVWPL LGVIDESLDE PWCATLATHL GHFEMGEEYE
LRQGRRYAVA RRLAGLFASY ARQRPQLLVD WDGLPDDLAW QKALWQALCE RIDADPPHIR
HAKTLVQLHE SPTDLPQRLS LFGHTRLPAT EVELLTALAT HHDLHLWLPH PSDTLWQALS
TRKGPLPRRE DTSHRDVGHP LLATLGRDLR EMQRLLPEPD TDEFRGRSEY PDTLLGWLQS
DIAADAVRPQ GRHHRREDRS IQVHSCHGPS RQIDVLREVL LGLLADDPTL EPRDILVMCP
DIETYAPLIT AGFGLGDVVP RTRGAHINLS AHPAHKLRVR LADRALVQTN PLLAVAAQLL
ALAGGRATAS EVLNLAESAP VRARFGFTDD DLDAITAWTR EANIRWGFDQ EHRRPYGVEF
LHNTWRFGID RVLAGVAMSD DSHAWLGTTL PLDDVSSNRV ELAGRFADFV EKLRRTVDQL
SGTRPLHEWL DALTAGIDAL ALADEDWPAA QMQREFAEIT ARAGDTATSL RLADVRALLD
RHLAGRPTRA NFRTGTLTVC TMVPMRSVPH RVVCLVGLDD GVFPRLGAVD GDDALARDPM
TGERDIRSED RQLLLDAILA ATQTLVITYT GANEYSGQAR PPAVPLAELI DTLKITTEDS
ALDVLTRHPL QPFDKRNVIP GALVPDEPFT FDQTALVAAR ASSGERAMRP AFFSDPLPPP
LPDDVALEDL LNFFKDPVKG FFRALDYTLP WDVEGVSDVM PVDIDALEEW TVGDRMLSDI
LRGMTPAAAQ QAEWRRGTLP PGQLGWRRAI ALRDQCALLA AEALGFRDTD GQAYDVDIDL
GGGRRLTGTV SPVFGDRLVS VTYSKLGGKH LLQSWIPLLA LAAGYPDRDW LAVCIGRPAR
GTTPRVEGLG GPDNPVDLLA DLVAIYDAGR REPLPLPVKT SYAWAEARHC GDDPEQKAGF
RWRSGRYPGE DAEPAHVRAW GRDAWLRDLM QPLRPGEEFE GETHRLGAYS SRLWLPLLRA
ERPVR
