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Database: UniProt
Entry: UVRC_LISMH
LinkDB: UVRC_LISMH
Original site: UVRC_LISMH 
ID   UVRC_LISMH              Reviewed;         603 AA.
AC   B8DHZ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, 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=LMHCC_1419;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(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; CP001175; ACK39764.1; -; Genomic_DNA.
DR   RefSeq; WP_012581489.1; NC_011660.1.
DR   AlphaFoldDB; B8DHZ8; -.
DR   SMR; B8DHZ8; -.
DR   KEGG; lmh:LMHCC_1419; -.
DR   HOGENOM; CLU_014841_3_2_9; -.
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; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR047296; GIY-YIG_UvrC_Cho.
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; PF12826; HHH_2; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR   SMART; SM00465; GIYc; 1.
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   SOS response.
FT   CHAIN           1..603
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000200592"
FT   DOMAIN          15..92
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          197..232
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   603 AA;  69318 MW;  8C9B70B4F58EAD30 CRC64;
     MSSEHIQNKL ALLPDQPGCY LMKDRQGTII YVGKAKILKN RVRSYFSGTH DSKTQRLVQE
     IVDFEYIVTS SNVEALLLEI NLIKKHDPRF NIRLKDDKTY PFIKITNERH PRLIITRQVK
     KDKGKYFGPY PNVYAANEVK RILDRLYPLR KCSTLPNKVC LYYHLGQCLA PCVFDVEASK
     YKEMQDEIVA FLNGGYKTVK NDLMKKMQEA AENMEFEKAG EFRDQINAIE TTMEKQKMTM
     NDFVDRDVFG YAIDKGWMCV QVFFIRQGKL IERDVSQFPF YNDADEDFLT FIGQFYQKAN
     HIPPKEIYLP DDVDSEAVQA VVPDTKIIVP QRGNKKDLVK LAYKNAKISL NEKFMLLERN
     EERTVGAVER LGEAMGIPTP SRVEAFDNSN IHGTDPVSAM VTFLDGKPSK NDYRKYKIKT
     VEGPDDYATM REVIRRRYWR VLKEGLPMPD LILIDGGKGQ IDSAKDVLTN ELGLDIPVAG
     LAKDDKHRTS QLLFGDPLEI VPLERNSQEF YLLQRMQDEV HRFAITFHRQ LRSKTGFQSI
     LDGIPGVGPG RKKKLLKHFG SMKKLKEASV EEIKEAGVPL NVAEEVHKHI TAFNEKAKNT
     EQK
//
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