UVRC_STAAW
ID UVRC_STAAW Reviewed; 593 AA.
AC Q8NX55;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=MW1029;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94894.1; -; Genomic_DNA.
DR RefSeq; WP_000390525.1; NC_003923.1.
DR AlphaFoldDB; Q8NX55; -.
DR SMR; Q8NX55; -.
DR EnsemblBacteria; BAB94894; BAB94894; BAB94894.
DR KEGG; sam:MW1029; -.
DR HOGENOM; CLU_014841_3_2_9; -.
DR OMA; HIECFDN; -.
DR Proteomes; UP000000418; 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; 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..593
FT /note="UvrABC system protein C"
FT /id="PRO_0000138342"
FT DOMAIN 17..94
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 199..234
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 593 AA; 68685 MW; BC2E8E1FAD71C60F CRC64;
MEDYKQRIKN KLNVVPMEPG CYLMKDRNDQ VIYVGKAKKL RNRLRSYFTG AHDAKTTRLV
GEIRRFEFIV TSSETESLLL ELNLIKQYQP RYNILLKDDK SYPFIKITKE KYPRLLVTRT
VKQGTGKYFG PYPNAYSAQE TKKLLDRIYP YRKCDKMPDK LCLYYHIGQC LGPCVYDVDL
SKYAQMTKEI TDFLNGEDKT ILKSLEERML TASESLDFER AKEYRDLIQH IQNLTNKQKI
MSSDKTIRDV FGYSVDKGWM CIQVFFIRQG NMIKRDTTMI PLQQTEEEEF YTFIGQFYSL
NQHILPKEVH VPRNLDKEMI QSVVDTKIVQ PARGPKKDMV DLAAHNAKVS LNNKFELISR
DESRTIKAIE ELGTQMGIQT PIRIEAFDNS NIQGVDPVSA MVTFIDGKPD KKNYRKYKIK
TVKGPDDYKS MREVVRRRYS RVLNEGLPLP DLIIVDGGKG HMNGVIDVLQ NELGLDIPVA
GLQKNDKHQT SELLYGASAE IVPLKKNSQA FYLLHRIQDE VHRFAITFHR QTRQKTGLKS
ILDDIDGIGN KRKTLLLRSF GSIKKMKEAT LEDFKNIGIP ENVAKNLHEQ LHK