ID   UVRC_CLOB1              Reviewed;         618 AA.
AC   A7FYX4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CLB_3436;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
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; CP000726; ABS33474.1; -; Genomic_DNA.
DR   RefSeq; WP_012048309.1; NC_009697.1.
DR   AlphaFoldDB; A7FYX4; -.
DR   SMR; A7FYX4; -.
DR   GeneID; 5186190; -.
DR   KEGG; cba:CLB_3436; -.
DR   HOGENOM; CLU_014841_3_2_9; -.
DR   OMA; HIECFDN; -.
DR   OrthoDB; 1036075at2; -.
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_1000099468"
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;  71685 MW;  52672BA7DDA19AA9 CRC64;
     MFDLEYQLKN LPDKPGVYLM KNNLGEIIYV GKAKILKNRV RQYFQKSQKH SEKVKAMVKN
     IEEFEYIITD SEIEALILEC NLIKKYRPKY NILLKDDKHY PFIKVTLAED FPRVISTRKV
     TKDGSKYFGP YVDGSSVKDI IELIKKTFPI RTCKKNIVEE AKAIRPCLNY QIGLCKAPCA
     QYIKKSEYRE TIDDVIKLLS GKHLDIVENF KLNMEKAAEN LEFEKAAMLR DKINIIEKIG
     EKQKIILNNF DNEDYISLYS DGKDTCFQVF FLRNGKIVGR EHFIIEDTFD TNSSTLISNF
     LKEFYGGTAY IPKTIYVPNI EDEALLEQWL TLKKESKSTI KIPIKGEKKN ILVLVEKNAK
     TTLENFKLKY LQEKALYDNV LKDLKNILRL QEEPIRIEAF DISNIQGFDS VGSMVVFEKG
     RAKPSDYRRF KINTVKGADD YKSMKEILTR RFQHGLSEIK SIQDRKLEFS SGKFSVFPDL
     ILMDGGKGQI NIALEVLNAF NIDIPVCGMV KDNKHRTRGL IYNGEEIIIN KYGSVMKFIT
     RVQDEVHRFA ISYHRSLRGK NSFHSLLDDI PNIGEKRKKD LLFNFKSIDN IKKATYEELL
     SIPSMDKKSA ECVLEFFK