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Database: UniProt
Entry: A0A098F044_9BACI
LinkDB: A0A098F044_9BACI
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ID   A0A098F044_9BACI        Unreviewed;       192 AA.
AC   A0A098F044;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cytochrome c oxidase Cu(A) center assembly protein {ECO:0000313|EMBL:CEG27543.1};
GN   ORFNames=BN1002_02410 {ECO:0000313|EMBL:CEG27543.1};
OS   Bacillus sp. B-jedd.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG27543.1, ECO:0000313|Proteomes:UP000042335};
RN   [1] {ECO:0000313|EMBL:CEG27543.1, ECO:0000313|Proteomes:UP000042335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-jedd {ECO:0000313|EMBL:CEG27543.1,
RC   ECO:0000313|Proteomes:UP000042335};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) 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; CCXR01000001; CEG27543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A098F044; -.
DR   STRING; 1476857.BN1002_02410; -.
DR   Proteomes; UP000042335; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000042335};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..192
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039716256"
FT   DOMAIN          27..192
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         65
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         69
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         156
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        65..69
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   192 AA;  21521 MW;  6136EF296128CC50 CRC64;
     MKIKALLLAM AAVVLVLSAC GPKEIKGAKN WPVEDFTFTN QDNKQFGLKD LEGKVWMADF
     IFTNCETVCP PMTANMAEIQ EMAAEEGIKN IEFVSFSVDP EGDTPEALKE YGTKFDADLK
     NWNFLTGYEQ EEIEEFAVKY FKTPVAMPKE GDQVVHGTSF FLVGKDGKIK TYYSGVSNVP
     YDDIIKDIKT LQ
//
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