UVRC_BORBZ
ID UVRC_BORBZ Reviewed; 603 AA.
AC B7J223;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=BbuZS7_0464;
OS Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=445985;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS7;
RX PubMed=20935092; DOI=10.1128/jb.01158-10;
RA Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA Mongodin E.F., Luft B.J.;
RT "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL J. Bacteriol. 193:1018-1020(2011).
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; CP001205; ACK74967.1; -; Genomic_DNA.
DR RefSeq; WP_002657940.1; NC_011728.1.
DR AlphaFoldDB; B7J223; -.
DR SMR; B7J223; -.
DR PRIDE; B7J223; -.
DR EnsemblBacteria; ACK74967; ACK74967; BbuZS7_0464.
DR GeneID; 56567889; -.
DR KEGG; bbz:BbuZS7_0464; -.
DR HOGENOM; CLU_014841_3_2_12; -.
DR OMA; HIECFDN; -.
DR OrthoDB; 1036075at2; -.
DR Proteomes; UP000006901; 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; 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; PF08459; UvrC_HhH_N; 1.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR TIGRFAMs; TIGR00194; uvrC; 1.
DR PROSITE; PS50164; GIY_YIG; 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..603
FT /note="UvrABC system protein C"
FT /id="PRO_1000200573"
FT DOMAIN 17..94
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 603 AA; 69833 MW; B9EDDDB6B4A63484 CRC64;
MKENLTNLFE KVIKLPTTSG CYKMLNENKK ILYIGKAKNL RSRVKSYFLE KNSHKIKILM
KNVKSIEVIT TNSEYEALLL ECNLIKTHKP DYNVKLKDGK GYPMVRITHE KYPRIFKTRK
IINDKSEYFG PFTNVKKLDQ VLDFINKTFK IRKCKKKSNA PCLYYHMGQC LGVCYKENLE
KEYQKELDKA KSILNGNISE ISSQIDIKLK HAIQKEDFET AIKLKEIRNS LIEINQIQIV
TKTNNLNIDY VHVHPGENVN TIIVLKYRNG KLVERDANFD ESICKENELI LQFLIQYYTS
INMIVPDKIH IFLKDIDTKN VEKLINEIKN TKTEIIYKET EEILKIMEMA ISNAELSLRE
YENKSTKALE SLKIVLEMDK LPKIIEGFDI AHLKGQETVA SMVTFKMGMP FKENYRLYKL
NSLLKGEIDD FKAIKEVISR RYSEIINNNL ELPNLILIDG GKGQLNAALS ILKGLKIENK
VKVCSLAKKQ ETIFLTTNKK GINLPQGHPA LRILQNVRDE AHRKANGFNK KRREKITLLY
TKIHGIGEKT AQKILKSIGT YKDILPLSEN EISEKIKVNV QLAKRIKEFA IKENSIKNNN
QDK