ID   UVRC_LEGPC              Reviewed;         618 AA.
AC   A5IAT1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=LPC_0494;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000675; ABQ54481.1; -; Genomic_DNA.
DR   RefSeq; WP_011947562.1; NC_009494.2.
DR   AlphaFoldDB; A5IAT1; -.
DR   SMR; A5IAT1; -.
DR   PRIDE; A5IAT1; -.
DR   KEGG; lpc:LPC_0494; -.
DR   HOGENOM; CLU_014841_3_0_6; -.
DR   OMA; HIECFDN; -.
DR   BioCyc; LPNE400673:LPC_RS14145-MON; -.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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   SMART; SM00278; HhH1; 2.
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_1000077802"
FT   DOMAIN          19..97
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          208..243
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   618 AA;  70465 MW;  8483F1E5ECA16BE0 CRC64;
     MNDLQLSAEL ALFLTKLPGE PGIYRMLDEE GTVLYVGKAA NLKKRVNSYF SKQNTGVKTR
     ALVSQIKSIE ISVTRSETEA LLLESNLIKA LRPKYNVLLR DDKSYPYIHL SNHPDFPRIE
     LYRSKKKPPS GNFFGPYPGV AAVRETIVTI QKIFKIRNCR DSYFKARSRP CLQYQIKRCT
     APCVHYISPE NYKLSVEDAI RFLQGKCQII LDELAERMKQ AVSQLNFEEA AVLRDQIKNL
     RLIQEQQGVV QLRGDADVIA IEVRPGFACI QCVTIREGQV LNSQSFFPTV PYAVLDEELD
     ANSLWQQTFE AFVGFYYLDT SERIPDLIIT NQSITESRSL EYILSQRRGK SCKIQVNPRG
     VKSRWMDFAV NNLRISVAEY VSKHSTIKSR YQALKQLLAL DKNIERMECF DISHTQGEST
     VASCVVFDTE GPRPSEYRRF NIEGITPGDD YAAMEQAVTR RFKRLIDAQL LPDVLIIDGG
     KGQVSIVKRV ITSLGVEDIT LLGVSKGPSR KAGWEKLILV NENREFVLPE DSKALHLLQH
     IRDEAHRFAI TAHRKKRQKT RVESTLESIE GVGTKRRQAL LQRFGGLREL AKAPLEEICK
     VQGINEQLAK RIYEHFHP