ID   RECC_MYCTU              Reviewed;        1097 AA.
AC   P9WIQ5; L0T7A5; P96921;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 43.
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=Rv0631c;
GN   ORFNames=MTCY20H10.12c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(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       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; AL123456; CCP43372.1; -; Genomic_DNA.
DR   PIR; D70612; D70612.
DR   RefSeq; NP_215145.1; NC_000962.3.
DR   RefSeq; WP_003900193.1; NZ_KK339370.1.
DR   AlphaFoldDB; P9WIQ5; -.
DR   SMR; P9WIQ5; -.
DR   STRING; 83332.Rv0631c; -.
DR   PaxDb; P9WIQ5; -.
DR   GeneID; 888008; -.
DR   KEGG; mtu:Rv0631c; -.
DR   TubercuList; Rv0631c; -.
DR   eggNOG; COG1330; Bacteria.
DR   OMA; SFDLMQY; -.
DR   PhylomeDB; P9WIQ5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0006310; P:DNA recombination; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1097
FT                   /note="RecBCD enzyme subunit RecC"
FT                   /id="PRO_0000087122"
SQ   SEQUENCE   1097 AA;  119501 MW;  D23908283F18D580 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 VHNTWRFGLD 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