ID   UVRC_ACIBY              Reviewed;         599 AA.
AC   B0VE41;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=ABAYE3465;
OS   Acinetobacter baumannii (strain AYE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYE;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM88255.1; -; Genomic_DNA.
DR   RefSeq; WP_012300759.1; NC_010410.1.
DR   AlphaFoldDB; B0VE41; -.
DR   SMR; B0VE41; -.
DR   EnsemblBacteria; CAM88255; CAM88255; ABAYE3465.
DR   GeneID; 66398707; -.
DR   KEGG; aby:ABAYE3465; -.
DR   HOGENOM; CLU_014841_3_0_6; -.
DR   OMA; HIECFDN; -.
DR   Proteomes; UP000002446; 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   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..599
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000099452"
FT   DOMAIN          18..96
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          207..242
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   599 AA;  67954 MW;  3959135D2DE94035 CRC64;
     MNQNARPHIE KILANLTQLP GVYKMLGKEG ELLYVGKAKN LKNRVSSYFV KTIEHPKTQA
     LVARIYDIET LVTRSETEAL LLEQNLIKQH RPPYNIMLRD DKSYVYIFVS ADKPYPRIAS
     GRGKGKHQIG KFFGPYPSAY SARDTLLVLQ KLFNVRQCEN SYFSQRKRPC LQYQIKRCSA
     PCVGLVSPED YKEDVNNSIR FLQGDTKELN QELIAKMEQA AADLEFEKAV FYRDRLSLLR
     EVQAQQAVFK VKGEADILAI AYQAGVTCVQ IMHVRNGRML GGKSYFPDML GDDLGQMLSD
     FMANFYFQVA DEVPSELIVN TALPDRKELE EALAQQFGKK VQIKSSVRET RAEWLELAEM
     NVQHAIKGQL SNHLELNERF HQLEQVVGRP IDRIECFDIS HTMGEAPIAS CVVFDQGGAR
     KRDYRQFAIQ DITAGDDYAA MRQALTRRYK KAMLPDLLLI DGGKGQLHMA MEVMQELGLE
     AFMVGVSKGE GRKPGLETLH FTDGTKIQLP EDSKALHLIQ QVRDEAHRFA ITKHRAKRDK
     RRSTSVLEAI PGLGPKRRRD LLTHFGGIQG VLKASEKELT VVPGLGEVMA RTIYKILHE