RECC_MYCTO
ID RECC_MYCTO Reviewed; 1097 AA.
AC P9WIQ4; L0T7A5; P96921;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
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=MT0659;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 recognizes the wild-type Chi sequence, and when added to isolated RecB
CC increases its ATP-dependent helicase processivity. {ECO:0000255|HAMAP-
CC Rule:MF_01486}.
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 -!- SIMILARITY: Belongs to the RecC family. {ECO:0000255|HAMAP-
CC Rule:MF_01486}.
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DR EMBL; AE000516; AAK44883.1; -; Genomic_DNA.
DR PIR; D70612; D70612.
DR RefSeq; WP_003917323.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIQ4; -.
DR SMR; P9WIQ4; -.
DR EnsemblBacteria; AAK44883; AAK44883; MT0659.
DR KEGG; mtc:MT0659; -.
DR PATRIC; fig|83331.31.peg.699; -.
DR HOGENOM; CLU_007513_1_0_11; -.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..1097
FT /note="RecBCD enzyme subunit RecC"
FT /id="PRO_0000427964"
SQ SEQUENCE 1097 AA; 119467 MW; 85C5305D184AA3BB CRC64;
MALHLHRAER TDLLADGLGA LLADPQPDPF AQELVLVAAR GVERWLSQRL SLVLGCGPGR
ADGVCAGIAF RNPQSLIAEI TGTLDDDPWS PEALAWPLLA VIDASLDEPW CRTLASHLGH
FATTDAEAEL RRGRRYSVAR RLAGLFASYA RQRPGLLAAW LDGDLGELPG DLAWQPPLWR
ALVTTVGADP PHVRHDKTIA RLRDGPADLP ARLSLFGHTR LACTDVQLLD ALAVHHDLHL
WLPHPSDELW RALAGFQGAD GLLPRRQDTS RRAAQHPLLE TLGRDVRELQ RALPAARATD
EFLGATTKPD TLLGWLQADI AGNAPRPAGR SLSDADRSVQ VHACHGPARQ IDVLREVLLG
LLEDDPTLQP RDIVVMCPDI DTYAPLIVAG FGLGEVAGDC HPAHRLRVRL ADRALTQTNP
LLSVAAELLT IAETRATASQ LLNLAQAAPV RAKFGFADDD LDTITTWVRE SNIRWGFDPT
HRRRYGLDTV VHNTWRLGLD RILTGVAMSE DSQAWLDTAL PLDDVGSNRV ELAGRLAEFV
ERLHHVVGGL SGARPLVAWL DALATGIDLL TACNDGWQRA QVQREFADVL ARAGSRAAPL
LRLPDVRALL DAQLAGRPTR ANFRTGTLTV CTMVPMRSVP HRVVCLVGLD DGVFPRLSHP
DGDDVLAREP MTGERDIRSE DRQLLLDAIG AATQTLVITY TGADERTGQP RPPAVPLAEL
LDALDQTTSA PVRERILVTH PLQPFDRKNV TPGALLGAKP FTFDPAALAA AQAAAGKRCP
PTAFISGRLP APPAADVTLA DLLDFFKDPV KGFFRALDYT LPWDVDTVED SIPVQVDALA
EWTVGERMLR DMLRGLHPDD AAHSEWRRGT LPPGRLGVRR AKEIRNRARD LAAAALAHRD
GHGQAHDVDV DLGDGRRLSG TVTPVFGGRT VSVTYSKLAP KHVLPAWIGL VTLAAQEPGR
EWSALCIGRS KTRNHIARRL FVPPPDPVAV LRELVLLYDA GRREPLPLPL KTSCAWAQAR
RDGQDPYPPA RECWQTNRFR PGDDDAPAHV RAWGPRAPFE VLLGKPRAGE EVAGEETRLG
ALAARLWLPL LAAEGSV
