UVRC_STAA1
ID UVRC_STAA1 Reviewed; 593 AA.
AC A7X172;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=SAHV_1137;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
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; AP009324; BAF78020.1; -; Genomic_DNA.
DR RefSeq; WP_000390524.1; NC_009782.1.
DR AlphaFoldDB; A7X172; -.
DR SMR; A7X172; -.
DR KEGG; saw:SAHV_1137; -.
DR HOGENOM; CLU_014841_3_2_9; -.
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..593
FT /note="UvrABC system protein C"
FT /id="PRO_1000077845"
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; 68687 MW; 6A15FEB13AE86780 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 FGYCVDKGWM CIQVFFIRQG NMIKRDTTMI PLQQTEEEEF YTFIGQFYSL
NQHILPKEVH VPRNLDKEMI QSVVDTKIVQ PARGPKKDMV DLAAHNAKVS LNNKFELISR
DESRTIKAIE ELGTQMGIQT PIRIEAFDNS NIQGVDPVSA MVTFVDGKPD KKNYRKYKIK
TVKGPDDYKS MREVVRRRYS RVLNEGLPLP DLIIVDGGKG HMNGVIDVLQ NELGLDIPVA
GLQKNDKHQT SELLYGASAE IVPLKKNSQA FYLLHRIQDE VHRFAITFHR QTRQKTGLKS
ILDDIDGIGN KRKTLLLRSF GSIKKMKEAT LEDFKNIGIP ENVAKNLHEQ LHK