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Database: UniProt
Entry: A0A096AIM7_9BURK
LinkDB: A0A096AIM7_9BURK
Original site: A0A096AIM7_9BURK 
ID   A0A096AIM7_9BURK        Unreviewed;       247 AA.
AC   A0A096AIM7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF2130_06230 {ECO:0000313|EMBL:KGF30557.1};
OS   Oligella urethralis DNF00040.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Oligella.
OX   NCBI_TaxID=1401065 {ECO:0000313|EMBL:KGF30557.1, ECO:0000313|Proteomes:UP000029629};
RN   [1] {ECO:0000313|EMBL:KGF30557.1, ECO:0000313|Proteomes:UP000029629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00040 {ECO:0000313|EMBL:KGF30557.1,
RC   ECO:0000313|Proteomes:UP000029629};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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:KGF30557.1}.
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DR   EMBL; JRNI01000023; KGF30557.1; -; Genomic_DNA.
DR   RefSeq; WP_036559155.1; NZ_JRNI01000023.1.
DR   AlphaFoldDB; A0A096AIM7; -.
DR   eggNOG; COG1999; Bacteria.
DR   OrthoDB; 9790194at2; -.
DR   Proteomes; UP000029629; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029629};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         122
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         126
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         211
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        122..126
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   247 AA;  27947 MW;  9078F5AD94C58C5D CRC64;
     MTLSPSIYQA LVFELCPGVT KHISSAWRRF NQQSEAARMR FVAYFLPLLI SLSVAFSLLA
     MRPVAAQWQH LFNLTHSDFN GSSIRGSHFG RGLEARDERG NDFRFDDFKG KLSLVYFGFT
     HCPDVCPNTL VQIQQALNLL APTEAEAVQF YFVTVDPARD TPQRLREYLS HFDPSFKALI
     AEPQQLQQIA KSFNVFYHQV PGPAGFYTME HSAYVFVLDK AAESVLLFSE GTPPDKMAAD
     LKKLLLE
//
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