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Database: UniProt
Entry: Q3KET6_PSEPF
LinkDB: Q3KET6_PSEPF
Original site: Q3KET6_PSEPF 
ID   Q3KET6_PSEPF            Unreviewed;       216 AA.
AC   Q3KET6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Putative SenC protein, required for cytochrome c oxidase activity {ECO:0000313|EMBL:ABA73720.1};
GN   OrderedLocusNames=Pfl01_1977 {ECO:0000313|EMBL:ABA73720.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA73720.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA73720.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA73720.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP000094; ABA73720.1; -; Genomic_DNA.
DR   RefSeq; WP_011333425.1; NC_007492.2.
DR   AlphaFoldDB; Q3KET6; -.
DR   KEGG; pfo:Pfl01_1977; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_4_2_6; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02968; SCO; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003782; SCO1/SenC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF25; SCO1 PROTEIN HOMOLOG; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..216
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004227491"
FT   BINDING         82
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        82..86
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   216 AA;  23539 MW;  30F150E606BC3DBA CRC64;
     MNRFASRGLL TLCLLAVGIQ QASAHSADEH AGHTAPAANS QEHAQVKFAD VPLLDQNGKT
     VHLEQDLVHN KIVVMSFIYT SCTTVCPVVS SIMGKVQKQL GARVGAEVQL VSISIDPQRD
     DPKRLQDYAR TFQKGPGWSW LTGSPQSISA TLKGLGSFSG DFKNHQPLIL VGDGNSRHWT
     RYYGFTDPAL LAKEVEKLSG LRTHAKHTAI AMEQQP
//
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