UVRC_BORDL
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 25-MAY-2022, entry version 70.
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; Spirochaetes; Spirochaetales; Borreliaceae; 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 RefSeq; WP_012538211.1; NC_011229.1.
DR AlphaFoldDB; B5RM14; -.
DR SMR; B5RM14; -.
DR STRING; 412419.BDU_455; -.
DR PRIDE; B5RM14; -.
DR EnsemblBacteria; ACH93400; ACH93400; BDU_455.
DR KEGG; bdu:BDU_455; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_2_12; -.
DR OMA; HIECFDN; -.
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 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; IPR010994; RuvA_2-like.
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; PF08459; UvrC_HhH_N; 1.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF82771; SSF82771; 1.
DR TIGRFAMs; TIGR00194; uvrC; 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