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Database: UniProt
Entry: A0A0S1YA14_9BORD
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Original site: A0A0S1YA14_9BORD 
ID   A0A0S1YA14_9BORD        Unreviewed;       207 AA.
AC   A0A0S1YA14;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Electron transporter {ECO:0000313|EMBL:ALM86875.1};
GN   ORFNames=ASB57_09975 {ECO:0000313|EMBL:ALM86875.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM86875.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM86875.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM86875.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) 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; CP013111; ALM86875.1; -; Genomic_DNA.
DR   RefSeq; WP_057656048.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1YA14; -.
DR   STRING; 1746199.ASB57_09975; -.
DR   Proteomes; UP000064621; Chromosome.
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; LDI DOMAIN-CONTAINING PROTEIN; 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:UP000064621};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..207
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006593027"
FT   DOMAIN          40..207
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         80
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         84
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         172
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        80..84
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   207 AA;  22037 MW;  388555BFC93D74DA CRC64;
     MPDMAARRGW SAWVLAAACL LPGALLGGLT ASAGAAQTVY DVAGHLPDLR FTLAGAQGKT
     VTDADVRGRT VLLFFGYANC PDVCPTTMAQ LTDVLGQLGE DAAKVRILFV SVDPHRDTPD
     ALQAYVNAFN HSAIGLTGTE KQIADLARRY RVSYQIDKPR PGADPEVYNV AHSRGVFVFD
     ATGRARLLLA DSADSAQIVQ SLKPLLK
//
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