UVRC_ECOLI
ID UVRC_ECOLI Reviewed; 610 AA.
AC P0A8G0; P07028; P76311; Q8XBD5;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=UvrABC system protein C;
DE Short=Protein UvrC;
DE AltName: Full=Excinuclease ABC subunit C;
GN Name=uvrC; OrderedLocusNames=b1913, JW1898;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6330676; DOI=10.1093/nar/12.11.4593;
RA Sancar G.B., Sancar A., Rupp W.D.;
RT "Sequences of the E. coli uvrC gene and protein.";
RL Nucleic Acids Res. 12:4593-4608(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3515318; DOI=10.1093/nar/14.5.2301;
RA Sharma S., Stark T.F., Beattie W.G., Moses R.E.;
RT "Multiple control elements for the uvrC gene unit of Escherichia coli.";
RL Nucleic Acids Res. 14:2301-2318(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=3295776; DOI=10.1093/nar/15.10.4273;
RA Moolenaar G.F., van Sluis C.A., Backendorf C., van de Putte P.;
RT "Regulation of the Escherichia coli excision repair gene uvrC. Overlap
RT between the uvrC structural gene and the region coding for a 24 kD
RT protein.";
RL Nucleic Acids Res. 15:4273-4289(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 604-610.
RX PubMed=3003065; DOI=10.1016/s0021-9258(17)36095-7;
RA Gopalakrishnan A.S., Chen Y.-C., Temkin M., Dowhan W.;
RT "Structure and expression of the gene locus encoding the
RT phosphatidylglycerophosphate synthase of Escherichia coli.";
RL J. Biol. Chem. 261:1329-1338(1986).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-399; ASP-438; ASP-466 AND HIS-538.
RC STRAIN=K12;
RX PubMed=1387639; DOI=10.1016/s0021-9258(19)37097-8;
RA Lin J.-J., Sancar A.;
RT "Active site of (A)BC excinuclease. I. Evidence for 5' incision by UvrC
RT through a catalytic site involving Asp399, Asp438, Asp466, and His538
RT residues.";
RL J. Biol. Chem. 267:17688-17692(1992).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ARG-42.
RX PubMed=10671556; DOI=10.1074/jbc.275.7.5120;
RA Verhoeven E.E., van Kesteren M., Moolenaar G.F., Visse R., Goosen N.;
RT "Catalytic sites for 3' and 5' incision of Escherichia coli nucleotide
RT excision repair are both located in UvrC.";
RL J. Biol. Chem. 275:5120-5123(2000).
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.
CC {ECO:0000269|PubMed:10671556, ECO:0000269|PubMed:1387639}.
CC -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X03691; CAA27329.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74980.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15733.1; -; Genomic_DNA.
DR EMBL; M24615; AAA24756.1; -; Genomic_DNA.
DR EMBL; X05398; CAA28983.1; -; Genomic_DNA.
DR EMBL; M12299; AAA98753.1; -; Genomic_DNA.
DR PIR; F64954; BVECUC.
DR RefSeq; NP_416423.4; NC_000913.3.
DR RefSeq; WP_001283421.1; NZ_STEB01000026.1.
DR PDB; 1KFT; NMR; -; A=554-610.
DR PDBsum; 1KFT; -.
DR AlphaFoldDB; P0A8G0; -.
DR SMR; P0A8G0; -.
DR BioGRID; 4260379; 105.
DR BioGRID; 851535; 1.
DR ComplexPortal; CPX-2153; UvrBC excinuclease repair complex.
DR DIP; DIP-47875N; -.
DR IntAct; P0A8G0; 47.
DR STRING; 511145.b1913; -.
DR jPOST; P0A8G0; -.
DR PaxDb; P0A8G0; -.
DR PRIDE; P0A8G0; -.
DR DNASU; 947203; -.
DR EnsemblBacteria; AAC74980; AAC74980; b1913.
DR EnsemblBacteria; BAA15733; BAA15733; BAA15733.
DR GeneID; 66674198; -.
DR GeneID; 947203; -.
DR KEGG; ecj:JW1898; -.
DR KEGG; eco:b1913; -.
DR PATRIC; fig|1411691.4.peg.337; -.
DR EchoBASE; EB1056; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_0_6; -.
DR InParanoid; P0A8G0; -.
DR OMA; HIECFDN; -.
DR PhylomeDB; P0A8G0; -.
DR BioCyc; EcoCyc:EG11063-MON; -.
DR BioCyc; MetaCyc:EG11063-MON; -.
DR EvolutionaryTrace; P0A8G0; -.
DR PRO; PR:P0A8G0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IDA:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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; 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; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Reference proteome; SOS response.
FT CHAIN 1..610
FT /note="UvrABC system protein C"
FT /id="PRO_0000138300"
FT DOMAIN 16..94
FT /note="GIY-YIG"
FT DOMAIN 204..239
FT /note="UVR"
FT MUTAGEN 42
FT /note="R->A: Defective in 3' incision but not in 5'
FT incision."
FT /evidence="ECO:0000269|PubMed:10671556"
FT MUTAGEN 399
FT /note="D->A,N: Defective in 5' incision but not in 3'
FT incision."
FT /evidence="ECO:0000269|PubMed:1387639"
FT MUTAGEN 438
FT /note="D->A,N: Defective in 5' incision but not in 3'
FT incision."
FT /evidence="ECO:0000269|PubMed:1387639"
FT MUTAGEN 466
FT /note="D->A,N: Defective in 5' incision but not in 3'
FT incision."
FT /evidence="ECO:0000269|PubMed:1387639"
FT MUTAGEN 538
FT /note="H->F,Y: Defective in 5' incision but not in 3'
FT incision."
FT /evidence="ECO:0000269|PubMed:1387639"
FT CONFLICT 291
FT /note="E -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:1KFT"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:1KFT"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:1KFT"
FT HELIX 579..584
FT /evidence="ECO:0007829|PDB:1KFT"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:1KFT"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:1KFT"
FT HELIX 599..608
FT /evidence="ECO:0007829|PDB:1KFT"
SQ SEQUENCE 610 AA; 68188 MW; F76766477C9ABCB6 CRC64;
MSDQFDAKAF LKTVTSQPGV YRMYDAGGTV IYVGKAKDLK KRLSSYFRSN LASRKTEALV
AQIQQIDVTV THTETEALLL EHNYIKLYQP RYNVLLRDDK SYPFIFLSGD THPRLAMHRG
AKHAKGEYFG PFPNGYAVRE TLALLQKIFP IRQCENSVYR NRSRPCLQYQ IGRCLGPCVE
GLVSEEEYAQ QVEYVRLFLS GKDDQVLTQL ISRMETASQN LEFEEAARIR DQIQAVRRVT
EKQFVSNTGD DLDVIGVAFD AGMACVHVLF IRQGKVLGSR SYFPKVPGGT ELSEVVETFV
GQFYLQGSQM RTLPGEILLD FNLSDKTLLA DSLSELAGRK INVQTKPRGD RARYLKLART
NAATALTSKL SQQSTVHQRL TALASVLKLP EVKRMECFDI SHTMGEQTVA SCVVFDANGP
LRAEYRRYNI TGITPGDDYA AMNQVLRRRY GKAIDDSKIP DVILIDGGKG QLAQAKNVFA
ELDVSWDKNH PLLLGVAKGA DRKAGLETLF FEPEGEGFSL PPDSPALHVI QHIRDESHDH
AIGGHRKKRA KVKNTSSLET IEGVGPKRRQ MLLKYMGGLQ GLRNASVEEI AKVPGISQGL
AEKIFWSLKH
