ID UVRC_GLUOX Reviewed; 645 AA.
AC Q5FNP1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=GOX2273;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW62006.1; -; Genomic_DNA.
DR RefSeq; WP_011253776.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FNP1; -.
DR SMR; Q5FNP1; -.
DR STRING; 290633.GOX2273; -.
DR KEGG; gox:GOX2273; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_0_5; -.
DR Proteomes; UP000006375; 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 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; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
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 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; PF14520; HHH_5; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00278; HhH1; 2.
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 Reference proteome; SOS response.
FT CHAIN 1..645
FT /note="UvrABC system protein C"
FT /id="PRO_0000264897"
FT DOMAIN 40..118
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 228..263
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 72520 MW; 458D4802F695B810 CRC64;
MTDLPPHSSH HPADQGEPLV PAEKKQGVEA IREALKTIPY SPGVYRMLSE KGEVLYVGKA
LSLKKRVSSY IRINQLPERL RRMVSMTVSM EIVITRTEAD ALLLEANYIK RMKPRFNILL
RDDKSYPWLM LTESHEFPQI TKQRGKPVKG ATYWGPFANA WAVNQTLNLV QRSFLLRSCS
DAVLNSRTRP CLLYQIKRCS APCVDRISKE DYAELVSEAR QFLSGHSTEL QQRLVAEMEQ
ASQELNYERA ASIRDRIRGF ASIQGSSTIN PTSINDADIM TIWQEAGQSC IQVFFIRGSR
NNGNRAFYPA HAEEETAADV LSAFMIQFYD NKPPPPSILV NCELPEPKLV EEALSIRRGQ
KVEILRPQRG EKKDVVEHAA LNAREALERK LAENTGQRRL LEGVAEVFGL PEIPQRIETY
DNSHIMGQAP YGVMVVGGPE GFNKRAYRKY AIKGPVTPGD DFGMMREVME RRFGHRSENG
ERPEDWPDLL LIDGGLGQFN AVRAVLADLG VTGIPIVAIA KGPDRDAGRE WFFTETKSPF
QLPPRDPVLY YLQRLRDEAH RFAITTHRAG RSKGLRSSEL DHVPGIGAAR KKALLNHFGS
AKSVRQASLE ELENAPGISS STATAIYGHF HPEWVQKTSA DNRSH
//
