ID   UVRC_CLOBM              Reviewed;         618 AA.
AC   B1L273;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE            Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE   AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN   Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=CLK_2812;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrC both incises the 5' and 3' sides of the
CC       lesion. The N-terminal half is responsible for the 3' incision and the
CC       C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-
CC       Rule:MF_00203}.
CC   -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC   -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00203}.
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DR   EMBL; CP000962; ACA56811.1; -; Genomic_DNA.
DR   RefSeq; WP_012344628.1; NC_010520.1.
DR   AlphaFoldDB; B1L273; -.
DR   SMR; B1L273; -.
DR   PRIDE; B1L273; -.
DR   EnsemblBacteria; ACA56811; ACA56811; CLK_2812.
DR   KEGG; cbl:CLK_2812; -.
DR   HOGENOM; CLU_014841_3_2_9; -.
DR   OMA; HIECFDN; -.
DR   Proteomes; UP000000722; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.340; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_00203; UvrC; 1.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR036876; UVR_dom_sf.
DR   InterPro; IPR004791; UvrC.
DR   InterPro; IPR001162; UvrC_RNase_H_dom.
DR   InterPro; IPR038476; UvrC_RNase_H_dom_sf.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF08459; UvrC_HhH_N; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   TIGRFAMs; TIGR00194; uvrC; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
DR   PROSITE; PS50151; UVR; 1.
DR   PROSITE; PS50165; UVRC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW   SOS response.
FT   CHAIN           1..618
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000099471"
FT   DOMAIN          13..92
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          204..239
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   618 AA;  71559 MW;  1760BE61632FB808 CRC64;
     MFDLEYQLKN LPDKPGVYLM KNNLGEIIYV GKAKILKNRV RQYFQKSQKH SEKVKAMVKN
     IEEFEYIITD SEIEALILEC NLIKKYRPKY NILLKDDKHY PFIKVTLAED FPRVISTRKV
     TKDGSKYFGP YVDGSSVKDI IELIKKTFPI RTCKKNIVEG AKAIRPCLNY QIGLCKAPCA
     QYIKKSEYRE IIDDVIKLLS GKHLDIVENF KLNMEKAAEN LEFEKAAMLR DKINIIEKIG
     EKQKIILNNF DNEDYISLYS DGKDTCFQVF FLRNGKIVGR EHFIIEDTFD TNSSTLISNF
     LKEFYGGTAY IPKTIYVPNI EDEALLEQWL TLKKESKSTI KIPIKGEKKN ILDLVEKNAK
     TTLENFKLKY LQEKALYDNV LKDLKNILSL QEEPIRIEAF DISNIQGFDS VGSMVVFEKG
     RAKPSDYRRF KISTVKGADD YKSMKEILTR RFQHGLSEIK SIQDRKLEFS SGKFSVFPDL
     ILMDGGKGQI NIALEVLNTF NIDIPVCGMV KDNKHRTRGL IYNGEEIIIN KYGSVMKFIT
     RVQDEVHRFA ISYHRSLRGK NSFHSLLDDI PNIGEKRKKD LLFNFKSIDN IKKATYEELL
     SIPSMDKKSA ESVLEFFK