ID   UVRC_PARPJ              Reviewed;         731 AA.
AC   B2SZU5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Bphyt_2889;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(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; CP001052; ACD17283.1; -; Genomic_DNA.
DR   RefSeq; WP_012433868.1; NC_010681.1.
DR   AlphaFoldDB; B2SZU5; -.
DR   SMR; B2SZU5; -.
DR   STRING; 398527.Bphyt_2889; -.
DR   EnsemblBacteria; ACD17283; ACD17283; Bphyt_2889.
DR   KEGG; bpy:Bphyt_2889; -.
DR   eggNOG; COG0322; Bacteria.
DR   HOGENOM; CLU_014841_3_0_4; -.
DR   OMA; HIECFDN; -.
DR   OrthoDB; 1036075at2; -.
DR   Proteomes; UP000001739; Chromosome 1.
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..731
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000099466"
FT   DOMAIN          21..99
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          208..243
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          346..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..366
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   731 AA;  79921 MW;  B97BE57A7AC9E05E CRC64;
     MTEPEATDAF EPKKVLAQLP HLPGVYRYYD THGAVLYVGK ARDLKKRVSS YFTKTLLSPR
     IAMMVTRIAR IETTVTRSEA EALLLENNLI KALAPRYNIL FRDDKSYPYL KLTGHKFPRM
     AYYRGAVDRK NQYFGPFPSA WAVRESIQIL QRVFQLRTCE DSVFNNRTRP CLLHQIGRCT
     APCVAAINEE DYARDVANAS RFLLGRQGEV MKELEQKMHA FASELKFEQA AAVRNQMSSL
     STVLHQQAIE VGSDSDVDIL AVVALGGRVC VNLAMVRGGR HLGDKAYFPA HVESALTADE
     GGLQEDDAAL ASVALASNSL AGDDVIDDET AALADTADAL AIAQEMPSED EENEQNDAAE
     EVDVAEEAGS EPAKPRKGRA ATGGIEAEVL EAFIAQHYLG NRVPPVLVVS HAPANRELVD
     VLIEQAGHKV TVLRQPQGQR RAWLTMAEQN ARLALARLLS EQGSQQARTR ALTDTLGMEC
     DDLAHLRIEC FDISHTMGEA TQASCVVYHH HKMQSSEYRR YNITGITPGD DYAAMRQVLT
     RRYEKMVEQA AANAADEAAE LQSDAAADPS LTPDAAEPVA AGGILPTIVL IDGGKGQVEI
     ARQVFTELGL DTGMLVGVAK GEGRKVGLET LIFADGRAPL ELGKESAALM LVAQIRDEAH
     RFAITGMRAK RGKTRQTSRL EELEGVGAKR RQRLLARFGG LRGVVAASVE DLASVEGISQ
     ALAEQIYRQL H