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Database: UniProt
Entry: A0A0F7M1P3_9GAMM
LinkDB: A0A0F7M1P3_9GAMM
Original site: A0A0F7M1P3_9GAMM 
ID   A0A0F7M1P3_9GAMM        Unreviewed;       222 AA.
AC   A0A0F7M1P3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein SCO1/SenC/PrrC, involved in biogenesis of respiratory and photosynthetic systems {ECO:0000313|EMBL:AKH68179.1};
GN   ORFNames=IMCC21906_00486 {ECO:0000313|EMBL:AKH68179.1};
OS   Spongiibacter sp. IMCC21906.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Spongiibacter.
OX   NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68179.1, ECO:0000313|Proteomes:UP000035013};
RN   [1] {ECO:0000313|EMBL:AKH68179.1, ECO:0000313|Proteomes:UP000035013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68179.1,
RC   ECO:0000313|Proteomes:UP000035013};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21906 belonging to the
RT   Gammaproteobacteria.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP011477; AKH68179.1; -; Genomic_DNA.
DR   RefSeq; WP_047010823.1; NZ_CP011477.1.
DR   AlphaFoldDB; A0A0F7M1P3; -.
DR   STRING; 1620392.IMCC21906_00486; -.
DR   KEGG; spoi:IMCC21906_00486; -.
DR   PATRIC; fig|1620392.3.peg.529; -.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000035013; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035013};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         96
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         100
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         185
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        96..100
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   222 AA;  25042 MW;  B55A58F87337EAA4 CRC64;
     MAGSENRANS QKQNRGIRLT VTIILVIASI LVGGFFYAFT KARVMTVDEL KAEGAYLYEN
     PRLLPKFSLV DDLGKSMGPK SLQGQWNLLF FGFTYCPDVC PTTLAQLKNF YQELDPEVQA
     NTQIWLVSVD PARDTPEQLH SYLEFFHPEF RGVTGEFLEI HRFATALNIP FSKVPGGGDN
     YMVDHSANIA LVNPKGHSMG FFKAPLEISR LTRTYLAIRE HY
//
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