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Database: UniProt
Entry: A0A1T4SZT1_9BACT
LinkDB: A0A1T4SZT1_9BACT
Original site: A0A1T4SZT1_9BACT 
ID   A0A1T4SZT1_9BACT        Unreviewed;       219 AA.
AC   A0A1T4SZT1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SKA33705.1};
GN   ORFNames=SAMN04488128_103880 {ECO:0000313|EMBL:SKA33705.1};
OS   Chitinophaga eiseniae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA33705.1, ECO:0000313|Proteomes:UP000190367};
RN   [1] {ECO:0000313|EMBL:SKA33705.1, ECO:0000313|Proteomes:UP000190367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA33705.1,
RC   ECO:0000313|Proteomes:UP000190367};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUWZ01000003; SKA33705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4SZT1; -.
DR   STRING; 634771.SAMN04488128_103880; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000190367; 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; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         91
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         95
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         180
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        91..95
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   219 AA;  24685 MW;  765B44968287CD0E CRC64;
     MRIRLWHILY SWQAAVITLI CLPLLAYSLV RWTEDRYAPL PFYGANNTVV SGPHDAARLP
     AFAFINQYGT TVTNTRLQQH ITIAHYFFTS CPAICPAMMQ QLQRVHAAFR NDTGICFVSL
     TVDPVRDSSA ALLRYGQRLS LPAQGWELLT GDKPSLYRFA RKGLYITATD GDGGPDDFIH
     SENIVLLDRQ QHIRGYYQGT SATATGQLIA DIKKLQHER
//
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