ID   UVRC_STRZP              Reviewed;         614 AA.
AC   C1CJ89;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=SPP_0632;
OS   Streptococcus pneumoniae (strain P1031).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=488223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1031;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000920; ACO21480.1; -; Genomic_DNA.
DR   RefSeq; WP_001061132.1; NC_012467.1.
DR   AlphaFoldDB; C1CJ89; -.
DR   SMR; C1CJ89; -.
DR   KEGG; spp:SPP_0632; -.
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..614
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000200605"
FT   DOMAIN          14..91
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          196..231
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          595..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  70437 MW;  E2EACE023C6D426F CRC64;
     MNNLIKSKLE LLPTSPGCYI HKDKNGTIIY VGKAKNLRNR VRSYFRGSHD TKTEALVSEI
     VDFEFIVTES NIEALLLEIN LIKENKPKYN IMLKDDKSYP FIKITNERYP RLIITRQVKK
     DGGLYFGPYP DVGAANEIKR LLDRIFPFRK CTNPPSKVCF YYHIGQCMAH TICKKDEAYF
     KSMAQEVSDF LKGQDDKIID DLKSKMAVAA QSMEFERAAE YRDLIQAIGT LRTKQRVMAK
     DLQNRDVFGY YVDKGWMCVQ VFFVRQGKLI ERDVNLFPYF NDPDEDFLTY VGQFYQEKSH
     LVPNEVLIPQ DIDEEAVKAL VDSKILKPQR GEKKQLVNLA IKNARVSLEQ KFNLLEKSVE
     KTQGAIENLG RLLQIPTPVR IESFDNSNIM GTSPVSAMVV FVNGKPSKKD YRKYKIKTVV
     GPDDYASMRE VIRRRYGRVQ REALTPPDLI VIDGGQGQVN IAKQVIQEEL GLDIPIAGLQ
     KNDKHQTHEL LFGDPLEVVD LSRNSQEFFL LQRIQDEVHR FAITFHRQLR SKNSFSSQLD
     GIDGLGPKRK QNLMRHFKSL TKIKEASVDE IVEVGVPRVV AEAVQRKLNP QGEALPQVAE
     ERVDYQTEGN HNEP