ID A6GVT4_FLAPJ Unreviewed; 241 AA.
AC A6GVT4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Probable cytochrome c oxidase biogenesis protein {ECO:0000313|EMBL:CAL42206.1};
DE EC=1.9.3.1 {ECO:0000313|EMBL:CAL42206.1};
GN OrderedLocusNames=FP0088 {ECO:0000313|EMBL:CAL42206.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL42206.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL42206.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; AM398681; CAL42206.1; -; Genomic_DNA.
DR RefSeq; YP_001295027.1; NC_009613.3.
DR AlphaFoldDB; A6GVT4; -.
DR STRING; 402612.FP0088; -.
DR EnsemblBacteria; CAL42206; CAL42206; FP0088.
DR KEGG; fps:FP0088; -.
DR PATRIC; fig|402612.5.peg.93; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_2_0_10; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Oxidoreductase {ECO:0000313|EMBL:CAL42206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006394};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 116
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 201
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 112..116
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 241 AA; 27975 MW; 9C5C6D062F174F51 CRC64;
MFLCLMLLLF CIFAKNTHVM LNFLRKFKTL FIVLSILSVI IISLFYNVLN RKTLPVFTPS
MVNPELVDST IQYVANKHII ANFAFTNQNG KIITQKDYAG KIYVADFFFT TCGTICPMMT
DNMVWLQDQI KDNPKVMLLS HSVTPDTDSV SVLKEYAQRK GVIDAKWNLV TGRKKDIYYI
ARKSYLAVKT GKPSELYDMV HTENFVLVDD KRRVRGFYDG TKREEVKRLL VDINWLLEKK
K
//
