UVRC_NITWN
ID UVRC_NITWN Reviewed; 689 AA.
AC Q3SPL2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 118.
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=Nwi_2526;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA05779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000115; ABA05779.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q3SPL2; -.
DR SMR; Q3SPL2; -.
DR STRING; 323098.Nwi_2526; -.
DR EnsemblBacteria; ABA05779; ABA05779; Nwi_2526.
DR KEGG; nwi:Nwi_2526; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_0_5; -.
DR Proteomes; UP000002531; 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 Reference proteome; SOS response.
FT CHAIN 1..689
FT /note="UvrABC system protein C"
FT /id="PRO_0000264918"
FT DOMAIN 83..161
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 271..306
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 75922 MW; C816CC93ECFA3A72 CRC64;
MTSDSSDTAK QIGSGQPSGS PADMRRRDGV APEQEVDPAS LETDEDDEAR LPDLPDEPVD
AVAEAPLAIG RAAIEHAVRH APTSPGVYRM MNAARDVLYV GKAKNVRKRL SSYARPTGQV
MRIARMIAAT AAVEIVSTGT ETEALLLEAN LIKQLRPRFN VQLRDDKSFP YILITGDHWA
PQLLKHRGAQ SRPGRYFGPF ASAGAVGRTI TALQRAFLVR SCTDSFFESR TRPCLLYQIK
RCAGPCTGEI DFPGYTALVR EATDFLSGRS RAVKEDLARA MEQAAADLAF ERAALYRDRL
AALSAIQSQQ GINPRTVEEA DVFAIHQEGG YFCVEVFFFR TGQNWGNRAY FPRAEKSFTP
EEVLGSFLAQ FYDDKPPPRL ILLSHRIEES ELLAHALSIK AGCKVVVSTP QRGEKKELVA
HALTNAREAL GRKLADTATQ SRLLQGLAAL LGLPQPPQRV EVYDNSHIQG ANAVGAMIVA
GPEGFLKNQY RKFNIRSESL TPGDDYAMMR EVLERRFKRL LTQKAADSRA AAEQDSAPQW
PDLVIIDGGL GQLNAARGVV DALGLSRVSL MAVAKGPDRD AGRETLFLPD RPAIKLEPRD
PVLYFIQRLR DEAHRFVIGS HRKLRRKDIR EAGLQEVPGI GPARKRALLH HFGTLKEIER
ASLADLGKVP GISAESARRI FDFFHARPA