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Database: UniProt
Entry: K2J8G0_9PROT
LinkDB: K2J8G0_9PROT
Original site: K2J8G0_9PROT 
ID   K2J8G0_9PROT            Unreviewed;       201 AA.
AC   K2J8G0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:EKE71503.1};
GN   ORFNames=P24_14704 {ECO:0000313|EMBL:EKE71503.1};
OS   Oceanibaculum indicum P24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Oceanibaculaceae; Oceanibaculum.
OX   NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE71503.1, ECO:0000313|Proteomes:UP000006746};
RN   [1] {ECO:0000313|EMBL:EKE71503.1, ECO:0000313|Proteomes:UP000006746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P24 {ECO:0000313|EMBL:EKE71503.1,
RC   ECO:0000313|Proteomes:UP000006746};
RX   PubMed=23209207; DOI=10.1128/JB.01859-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL   J. Bacteriol. 194:6942-6942(2012).
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:EKE71503.1}.
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DR   EMBL; AMRL01000023; EKE71503.1; -; Genomic_DNA.
DR   RefSeq; WP_008945544.1; NZ_AMRL01000023.1.
DR   AlphaFoldDB; K2J8G0; -.
DR   STRING; 1207063.P24_14704; -.
DR   PATRIC; fig|1207063.3.peg.2964; -.
DR   eggNOG; COG1999; Bacteria.
DR   Proteomes; UP000006746; 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:SF5; AT19154P; 1.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   Pfam; PF02630; SCO1-SenC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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:UP000006746}.
FT   DOMAIN          39..201
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         167
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        77..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   201 AA;  22416 MW;  F3A0EF8C63470110 CRC64;
     MSSTLLRRAL LIFIAGALVL LVALAGRVYM MMQQDAPQGT AALIGGPFEL VDQDGKPRRD
     SDFRGQYMLV NFGYTYCPDV CPLGLQVMAQ AMDMLPEEKA QKLTPIFITV DPARDTVEQM
     KNYVGFFHPR MVGLTGTPEQ VATAAKAYRV YYKKVESESA ADYLMDHSAI IYLMGPDGKY
     LANFTHETPP ERMAETLNKM L
//
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