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Database: UniProt
Entry: A0A1I0I8P3_9BACI
LinkDB: A0A1I0I8P3_9BACI
Original site: A0A1I0I8P3_9BACI 
ID   A0A1I0I8P3_9BACI        Unreviewed;       199 AA.
AC   A0A1I0I8P3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SET92747.1};
GN   ORFNames=SAMN05421676_11131 {ECO:0000313|EMBL:SET92747.1};
OS   Salinibacillus kushneri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX   NCBI_TaxID=237682 {ECO:0000313|EMBL:SET92747.1, ECO:0000313|Proteomes:UP000199095};
RN   [1] {ECO:0000313|EMBL:SET92747.1, ECO:0000313|Proteomes:UP000199095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SET92747.1,
RC   ECO:0000313|Proteomes:UP000199095};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOHJ01000011; SET92747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0I8P3; -.
DR   STRING; 237682.SAMN05421676_11131; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000199095; Unassembled WGS sequence.
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   InterPro; IPR013766; Thioredoxin_domain.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..199
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038685030"
FT   DOMAIN          35..198
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         73
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         161
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        73..77
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   199 AA;  22465 MW;  9925B10DCBF57679 CRC64;
     MKTKTTLFVL LTAFLFILSA CGADEENKSS QDYEGSLDIE VQDFTATNQD NKEMNLEDLK
     GTFWVADFIY TQCPDVCLTM TPNMAKLQNM VNDEGLDTRF VSFSVDPSVD TPEILKKYGQ
     NYDADFSTWD FLTGYSQKDI ESFAADSFKT LVSKVDDQVT HGTSFYLVAP NGHVINKYNG
     LKPEGVENLV SDMKRYQNQ
//
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