ID   M6ZK39_LEPIR            Unreviewed;       279 AA.
AC   M6ZK39;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=SCO1/SenC {ECO:0000313|EMBL:EMP04487.1};
GN   ORFNames=LEP1GSC124_0015 {ECO:0000313|EMBL:EMP04487.1};
OS   Leptospira interrogans serovar Pyrogenes str. 200701872.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1193029 {ECO:0000313|EMBL:EMP04487.1, ECO:0000313|Proteomes:UP000012117};
RN   [1] {ECO:0000313|EMBL:EMP04487.1, ECO:0000313|Proteomes:UP000012117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200701872 {ECO:0000313|EMBL:EMP04487.1,
RC   ECO:0000313|Proteomes:UP000012117};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA   Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-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:EMP04487.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AKWN02000524; EMP04487.1; -; Genomic_DNA.
DR   AlphaFoldDB; M6ZK39; -.
DR   BioCyc; LINT1193029:G11R4-4034-MONOMER; -.
DR   Proteomes; UP000012117; 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:SF8; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        246..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         90
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         179
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        86..90
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   279 AA;  31847 MW;  7BE6FC95664E575F CRC64;
     MAFRKSLISG IAFCLLTVSI YSYDPAARFD KNEKPKELEG VGVQEKLGNQ LDLSLSFRDE
     TGKSILLSSF FKRDKPVLLS LVYYKCPTLC NFHLNGVTDV LKKLSWEVGN EFEYVAVSFD
     PKETFDLASA KKNAYLKEYA RGNGQGWHFL TGDQKEITAL AESVGFSYKW NSENEQWIHS
     SVAYIITPSG KISRYLHGIT FDERTLKLSL LEASDGKIGD FTDQFALFCF QFDPGKNTYT
     LYAYNIMKLG GFFTLLIMAA FLIPFWIRHN RNSELIRKE
//