UVRC_BACSU
ID UVRC_BACSU Reviewed; 590 AA.
AC P14951;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
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=BSU28490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2559145; DOI=10.1099/00221287-135-11-2931;
RA Chen N.-Y., Zhang J.-J., Paulus H.;
RT "Chromosomal location of the Bacillus subtilis aspartokinase II gene and
RT nucleotide sequence of the adjacent genes homologous to uvrC and trx of
RT Escherichia coli.";
RL J. Gen. Microbiol. 135:2931-2940(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 382 AND C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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; J03294; AAA87316.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99578.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14809.2; -; Genomic_DNA.
DR PIR; A37192; A37192.
DR RefSeq; NP_390727.2; NC_000964.3.
DR RefSeq; WP_003246045.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P14951; -.
DR SMR; P14951; -.
DR STRING; 224308.BSU28490; -.
DR PaxDb; P14951; -.
DR PRIDE; P14951; -.
DR EnsemblBacteria; CAB14809; CAB14809; BSU_28490.
DR GeneID; 937729; -.
DR KEGG; bsu:BSU28490; -.
DR PATRIC; fig|224308.179.peg.3094; -.
DR eggNOG; COG0322; Bacteria.
DR InParanoid; P14951; -.
DR OMA; HIECFDN; -.
DR PhylomeDB; P14951; -.
DR BioCyc; BSUB:BSU28490-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
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; 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 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 Reference proteome; SOS response.
FT CHAIN 1..590
FT /note="UvrABC system protein C"
FT /id="PRO_0000138288"
FT DOMAIN 14..91
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 196..231
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT CONFLICT 382
FT /note="E -> V (in Ref. 1; AAA87316 and 2; CAA99578)"
FT /evidence="ECO:0000305"
FT CONFLICT 578..590
FT /note="AAAAQLLYDKLQK -> QRRLSSFTTNCKNNVVLLNKI (in Ref. 1;
FT AAA87316 and 2; CAA99578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 68472 MW; ECB6DE521F13E75A CRC64;
MNKQLKEKLA LLPDQPGCYL MKDRQQTVIY VGKAKVLKNR VRSYFTGSHD AKTQRLVTEI
EDFEYIVTSS NLEALILEMN LIKKHDPKYN VMLKDDKTYP FIKLTHERHP RLIVTRNVKK
DKGRYFGPYP NVQAARETKK LLDRLYPLRK CSKLPDRVCL YYHLGQCLAP CVKDISEETN
RELVESITRF LRGGYNEVKK ELEEKMHEAA ENLEFERAKE LRDQIAHIES TMEKQKMTMN
DLVDRDVFAY AYDKGWMCVQ VFFIRQGKLI ERDVSMFPLY QEADEEFLTF IGQFYSKNNH
FLPKEILVPD SIDQSMIEQL LETNVHQPKK GPKKELLMLA HKNAKIALKE KFSLIERDEE
RSIGAVQKLG EALNIYTPHR IEAFDNSNIQ GTNPVSAMIV FIDGKPYKKE YRKYKIKTVT
GPDDYGSMRE VVRRRYTRVL RENLPLPDLI IIDGGKGQIN AARDVIENEL GLDIPIAGLA
KDEKHRTSNL LIGDPLEVAY LERNSQEFYL LQRIQDEVHR FAISFHRQIR GKSAFQSVLD
DIPGIGEKRK KMLLKHFGSV KKMKEASLED IKKAGVPAAA AQLLYDKLQK
