ID F0J338_ACIMA Unreviewed; 240 AA.
AC F0J338;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Electron transport transmembrane protein Sco1/SenC/PrrC {ECO:0000313|EMBL:GAN73998.1};
DE SubName: Full=SenC protein {ECO:0000313|EMBL:BAJ81984.1};
GN OrderedLocusNames=ACMV_26370 {ECO:0000313|EMBL:BAJ81984.1};
GN ORFNames=Apmu_0130_23 {ECO:0000313|EMBL:GAN73998.1};
OS Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS 301).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ81984.1, ECO:0000313|Proteomes:UP000007100};
RN [1] {ECO:0000313|EMBL:BAJ81984.1, ECO:0000313|Proteomes:UP000007100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:BAJ81984.1}, and DSM 11245 / JCM 8867
RC / AIU301 {ECO:0000313|Proteomes:UP000007100};
RA Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA Hosoyama A., Yamada R., Fujita N.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAN73998.1, ECO:0000313|Proteomes:UP000032662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIU301 {ECO:0000313|EMBL:GAN73998.1,
RC ECO:0000313|Proteomes:UP000032662};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL Submitted (NOV-2012) 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; AP012035; BAJ81984.1; -; Genomic_DNA.
DR EMBL; BANA01000128; GAN73998.1; -; Genomic_DNA.
DR RefSeq; WP_013640732.1; NZ_BANA01000128.1.
DR AlphaFoldDB; F0J338; -.
DR KEGG; amv:ACMV_26370; -.
DR HOGENOM; CLU_1154430_0_0_5; -.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000007100; Chromosome.
DR Proteomes; UP000032662; Unassembled WGS sequence.
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:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 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 Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:GAN73998.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 115
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 115..119
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 240 AA; 26117 MW; F7F2981342F7658B CRC64;
MTDRSEYSDY QPRRGHRIGR RIAIGGAIGL GAALTAIAID PGIIGVTEHN TLETLAHLLG
WSRPHGRLAT TTDSAISPGA PIGGPFTLTN QFGQAMTPAS FRGRWMLVYF GYSRCPDDCP
LTLEKMAIMM NALGKLAKHV APVFITVDPT HDTPAVLRTY LPKFSNKIIG LTGPVPEIAK
VAREYDAYFN TTDHEASGQS LISHSTFIYL MAPNGKFENL FPVSITVPQL VHIMKKAIAQ
//
