SENC_RHOCB
ID SENC_RHOCB Reviewed; 221 AA.
AC Q52720; D5AKG7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein SenC;
GN Name=senC; OrderedLocusNames=RCAP_rcc00044;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=7592491; DOI=10.1128/jb.177.23.6958-6965.1995;
RA Buggy J., Bauer C.E.;
RT "Cloning and characterization of senC, a gene involved in both aerobic
RT respiration and photosynthesis gene expression in Rhodobacter capsulatus.";
RL J. Bacteriol. 177:6958-6965(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Involved in both aerobic respiration and photosynthesis gene
CC expression.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
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DR EMBL; L12050; AAA85464.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE83809.1; -; Genomic_DNA.
DR RefSeq; WP_013065791.1; NC_014034.1.
DR AlphaFoldDB; Q52720; -.
DR SMR; Q52720; -.
DR STRING; 272942.RCAP_rcc00044; -.
DR EnsemblBacteria; ADE83809; ADE83809; RCAP_rcc00044.
DR GeneID; 31489001; -.
DR KEGG; rcp:RCAP_rcc00044; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_1_5; -.
DR OMA; KHAGRDY; -.
DR OrthoDB; 1994201at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; IMP:CACAO.
DR CDD; cd02968; SCO; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper; Metal-binding; Photosynthesis; Reference proteome.
FT CHAIN 1..221
FT /note="Protein SenC"
FT /id="PRO_0000173874"
FT DOMAIN 45..210
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT CONFLICT 179..180
FT /note="Missing (in Ref. 1; AAA85464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 23211 MW; 825D1A298B02533E CRC64;
MNVSSKTAAL AATAAVVVVV GISAAVTLVP HETDRFAACR KGTGSASAQI GGPFTLISET
GATVTDRDVI TKPSLVYFGY SYCPDVCPID STRNAAAVDL LAERGHDVTP VFISVDAARD
TPPVLTEFTD LMSPKMIGLT GTPEQIDAAV KAYRAYYLIR NPGDPATLVD HSTQTYLMDP
KLGFLDFYDR DATPEMVADS VGCFLDALQT PGDTPAAGNG N