ID   UVRC_CAMJR              Reviewed;         600 AA.
AC   Q5HTL6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=CJE1382;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW35702.1; -; Genomic_DNA.
DR   RefSeq; WP_002898461.1; NC_003912.7.
DR   AlphaFoldDB; Q5HTL6; -.
DR   SMR; Q5HTL6; -.
DR   KEGG; cjr:CJE1382; -.
DR   HOGENOM; CLU_014841_3_2_7; -.
DR   OMA; HIECFDN; -.
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; 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; 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..600
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_0000227409"
FT   DOMAIN          15..100
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          203..238
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   600 AA;  69690 MW;  17075CEFA9AD8971 CRC64;
     MIKENLENEL KTLPNSAGVY QYFNQEGKLL YVGKAKNLKN RVKSYFAFTP NLHANPRNSL
     RIQKMIEETV HLEFIATNSE ADALILENSF IKQLHPKYNI LLRDDKTYPY IYVDFEEEFP
     RFEITRKLVK KSKIKYFGPF FKGARELLDA LYLYYPLKQK ASCKSPCIFY QISRCLAPCD
     KLISREKYLE ILDEAIHALL NPSVLLKNLE KQMLVLAQNE NYEEAAKVRD QIAMIKDLEV
     KVEIDIAKLE DFEVFALAFK NSVLSTLRFV VQNGKIISAN SKITPIRNDI QWDQNEIYKQ
     LILENFSMDI PLLANVIYVY EEFEDRVLLE EILSQRFDKK ISIKIPKIGE KRRICDLAFQ
     NALLNIEKEQ KNHDFTIQKE LKFYFELENL PNDIEIFDNS HLQGVANVGA MVTYRINSWD
     KSKYRKFHLK HKNDYDQMRE VLTRRALDFD KIPPPDLWLI DGGKALLDLA KEIIVSSGAN
     VDILAISKEK IDAKAHRAKG GAKDKIHSLK GEFSLSINDK KLQFLQKLRD EAHRFAISFH
     QNTKKKQDLK SSKLANLGLS SGVIQKLLAY YGNFESIYKA DFKDLTMLVG RKAAQKIKEN