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Database: UniProt
Entry: B5RM14
LinkDB: B5RM14
Original site: B5RM14 
ID   UVRC_BORDL              Reviewed;         602 AA.
AC   B5RM14;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
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=BDU_455;
OS   Borrelia duttonii (strain Ly).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borrelia.
OX   NCBI_TaxID=412419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ly;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(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; CP000976; ACH93400.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5RM14; -.
DR   SMR; B5RM14; -.
DR   STRING; 412419.BDU_455; -.
DR   KEGG; bdu:BDU_455; -.
DR   eggNOG; COG0322; Bacteria.
DR   HOGENOM; CLU_014841_3_2_12; -.
DR   OrthoDB; 9804933at2; -.
DR   Proteomes; UP000000611; 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; 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; IPR010994; RuvA_2-like.
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; PF08459; UvrC_RNaseH_dom; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS50164; GIY_YIG; 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..602
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000099460"
FT   DOMAIN          17..94
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          199..234
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   602 AA;  70225 MW;  C617135A0705D6AE CRC64;
     MRKHLNDLYK QIEKFPKTSG CYKMYSKDNK ILYIGKAKNL RSRVKNYFSK RTSHKTKILM
     NNVTNIEIIT TNSEYEALLL ECNLIKKYKP TYNIKLKDDK GYPMIRITCE KYPRIFKTRK
     IINDGSEYFG PYVNVKNLDL VLDLINKTFK TKKCKKKSKN PCLYFHMGQC LGVCYREDLE
     DEYRKEIEQI KHILNGNISK LLNDIEIKMK EVIMKENFEA AIKLKETKKS LIEISQTQII
     TKIDKLSEDY LYIHKTNSLN TIVILKYKDG KLTEKDIHFD ESIYEEDELI EKFITQYYTS
     PNMIVPDKIH IFKKIDTSNI TKLINELKNI KTEIIYKETQ DNIKIIEMAT SNAKLALITY
     NHEKNKAIEN LKTILEMKKL PKTIEGFDIA HINGYKTVAS LVTFKMGKPF KDGYRVYKIN
     SLSNGEIDDC KAIKEVISRR YSKLINEQLK LPDLILIDGG KGQLNAAYSI LKGLRIEEKI
     AICALAKKEE IIFLPNKNQG IKLQKRNSAL QVLQNVRDEA HRRANNFNNK LHNNIKLNYT
     KIKGIGEQKA KKILKVLGTY KDILLLNEDE IATKMKINIT MANKIKKFAE EQNLNNKQNN
     HI
//
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