ID   UVRC_BURM9              Reviewed;         747 AA.
AC   A2SA04;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
GN   OrderedLocusNames=BMA10229_A2824;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(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; CP000546; ABN01813.1; -; Genomic_DNA.
DR   RefSeq; WP_004192853.1; NC_008836.1.
DR   AlphaFoldDB; A2SA04; -.
DR   SMR; A2SA04; -.
DR   EnsemblBacteria; ABN01813; ABN01813; BMA10229_A2824.
DR   GeneID; 56596335; -.
DR   KEGG; bml:BMA10229_A2824; -.
DR   HOGENOM; CLU_014841_3_0_4; -.
DR   OMA; HIECFDN; -.
DR   Proteomes; UP000002283; Chromosome I.
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; 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   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW   SOS response.
FT   CHAIN           1..747
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000077760"
FT   DOMAIN          22..100
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          209..244
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          363..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  80836 MW;  8EB63B0873D50FA8 CRC64;
     MTSPDAPESR FEPKPILAQL PHLPGVYRYY DVQDAVLYVG KARDLKKRVS SYFTKTQLSP
     RIAMMITRIA RIETTVTRSE AEALLLENNL IKALAPRYNI LFRDDKSYPY LKLTGHRFPR
     MAYYRGAVDK KNQYFGPFPS AWAVRESIQI LQRVFQLRTC EDSVFNNRTR PCLLHQIGRC
     SAPCVGAIGE EDYARDVDNA SRFLLGRQGE VMGELERKMH AFAAELKFEQ AAAVRNQMSS
     LAKVLHQQAI DVGGDSDVDI LAVVAQGGRV CVNLAMVRGG RHLGDKAYFP AHVETALALA
     GDIEALAGEG AGDGVQAAAQ PAQAPLATDA DATDAAATEA KTVTAAAAAR AGARTAQAAG
     ARAAASAEGD VERRAEGETH ARADAREAAA LPDGAAAAQE ADADVDAAPL ETEVLEAFIA
     QHYLGNRVPP VLVVSHAPAN RELIDLLVEQ AGHKVAVVRQ PQGQKRAWLT MAEQNARLAL
     ARLLSEQGSQ QARTRSLADV LGYESDDLAQ LRIECFDISH TMGEATQASC VVYHHHRMQS
     SEYRRYNIAG ITPGDDYAAM RQVLTRRYEK MVEEAAAEAS ADEAAGIDGN AVHAAASAGR
     LPNVVLIDGG RGQVEIARQV FSELGLDISM LVGVAKGEGR KVGLETLIFA DGRAPLELGK
     ESAALMLVAQ IRDEAHRFAI TGMRAKRAKT RQTSRLEELE GVGAKRRQRL LARFGGLRGV
     VAASVDELAS VEGISRALAE QIYRQLH