ID   A0A0A8X5M0_9BACI        Unreviewed;       194 AA.
AC   A0A0A8X5M0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cytochrome oxidase biogenesis protein Sco1/senc/PrrC, putative copper metallochaperone {ECO:0000313|EMBL:GAM15280.1};
GN   ORFNames=SAMD00020551_3436 {ECO:0000313|EMBL:GAM15280.1};
OS   Mesobacillus selenatarsenatis SF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM15280.1, ECO:0000313|Proteomes:UP000031014};
RN   [1] {ECO:0000313|EMBL:GAM15280.1, ECO:0000313|Proteomes:UP000031014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF-1 {ECO:0000313|EMBL:GAM15280.1,
RC   ECO:0000313|Proteomes:UP000031014};
RA   Kuroda M., Sei K., Yamashita M., Ike M.;
RT   "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAM15280.1}.
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DR   EMBL; BASE01000079; GAM15280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8X5M0; -.
DR   STRING; 1321606.SAMD00020551_3436; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000031014; 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:UP000031014};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..194
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002042553"
FT   DOMAIN          29..194
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         71
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         158
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        67..71
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   194 AA;  21910 MW;  C418F7D03A4DDB90 CRC64;
     MILKKVFTLL MLAAVIIFAA GCGNSGLKDA KNYPIEDFTF TNQDGESVSK ADLEGKVWMA
     SFIFTNCADV CPPMTANMSK LQDRIKEEGL KDVEIVSFSV DPAVDNPEAL KEYGKKFNVD
     FKNWSFLTGY TQEEIEKFAL ENFKTLVKKP ETGDQVIHGT DFYLVDQNGD MRKYYTGLKE
     VPFEQIIEDI KALQ
//