ID UVRC_PASMU Reviewed; 608 AA.
AC P57882;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 27-MAR-2024, entry version 139.
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=PM0857;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK02941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004439; AAK02941.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_032854373.1; NC_002663.1.
DR AlphaFoldDB; P57882; -.
DR SMR; P57882; -.
DR STRING; 272843.PM0857; -.
DR EnsemblBacteria; AAK02941; AAK02941; PM0857.
DR KEGG; pmu:PM0857; -.
DR PATRIC; fig|272843.6.peg.867; -.
DR HOGENOM; CLU_014841_3_2_6; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000000809; 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 CDD; cd10434; GIY-YIG_UvrC_Cho; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR Gene3D; 3.30.420.340; UvrC, RNAse H endonuclease domain; 1.
DR HAMAP; MF_00203; UvrC; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
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 NCBIfam; TIGR00194; uvrC; 1.
DR PANTHER; PTHR30562:SF1; UVRABC SYSTEM PROTEIN C; 1.
DR PANTHER; PTHR30562; UVRC/OXIDOREDUCTASE; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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 Reference proteome; SOS response.
FT CHAIN 1..608
FT /note="UvrABC system protein C"
FT /id="PRO_0000138325"
FT DOMAIN 13..91
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 201..236
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 608 AA; 68946 MW; A021B63EB460E77A CRC64;
MFDAKSFLAN VSHDAGVYRM YDEKDTVIYV GKAKDLKKRL SSYFRTHLSS KKTEALVSAI
ARIDTTITSS ETEALLLEHN YIKTYQPRYN VLLRDDKSYP YILLTAERHP RISAYRGSKK
IKGEYFGPYP HASAVRETLS LLQKLFPIRQ CENAVYNNRS RPCLQYQIGR CAAPCVAGYV
TDEAYLQQVE LARLFLQGKD QQVLEHLIHK MEQASLALDF EEAARIRDQI QAVRAVMEKQ
FVSTERLDDM DILSIAYQLG IACVQVLFIR QGKMLGNRSY FPKVPANTTL SELTATFVGQ
FYLQAHQGRS IPHRIIVDHK LSEKTELEEL LTQQAGRKVH IQDNTKGEKS KYLQLAKMNA
QSALVTQLKQ STLLKERYQA LQAILQLGEI RRMECFDISH TMGEQTIASC VVFNQDGPLK
SDYRRFNITG ITAGDDYAAM EQALLKRYDK PLEQEKIPDV IFIDGGKGQL NRALQTFSKL
NVKWDKNQPH LIGVAKGIDR KAGLETLILS KQGKILHLPS DHLALHLIQH IRDESHQHAI
SGHRKKRQQA FLQSGLESVE GVGAKRRQTL LKYLGGMQGV KKATLDEIAS VPGISKALAE
RIYDALRD
//
