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Database: UniProt
Entry: M6JPP6_9LEPT
LinkDB: M6JPP6_9LEPT
Original site: M6JPP6_9LEPT 
ID   M6JPP6_9LEPT            Unreviewed;       279 AA.
AC   M6JPP6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=SCO1/SenC {ECO:0000313|EMBL:EMN23731.1};
GN   ORFNames=LEP1GSC063_1448 {ECO:0000313|EMBL:EMN23731.1};
OS   Leptospira santarosai serovar Arenal str. MAVJ 401.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049976 {ECO:0000313|EMBL:EMN23731.1, ECO:0000313|Proteomes:UP000012106};
RN   [1] {ECO:0000313|EMBL:EMN23731.1, ECO:0000313|Proteomes:UP000012106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAVJ 401 {ECO:0000313|EMBL:EMN23731.1,
RC   ECO:0000313|Proteomes:UP000012106};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA   van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA   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:EMN23731.1}.
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DR   EMBL; AHMU02000001; EMN23731.1; -; Genomic_DNA.
DR   RefSeq; WP_004469271.1; NZ_AHMU02000001.1.
DR   AlphaFoldDB; M6JPP6; -.
DR   Proteomes; UP000012106; 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;  31879 MW;  18215B382C9D1A14 CRC64;
     MVFKNSLITG IAFCLFTTSL LSYDPAVRFD KNEKPKELEG VGVQEKLGNQ LDLSLSFRDE
     TGKLVLLSSF FKKDKPVLLS LVYYKCPTLC NFHLNGITDV LKKLSWEVGK EFEYVAVSFD
     PKETFDLAHA KKNAYLKEYS RGDGQGWHFL TGNQKEIATL ADSVGFSYKW NPENEQWIHS
     SVAYVITPSG KISRYLHGVT FDERTLKLSL LEASDGKIGD FADQFALFCF QFDPGKNTYT
     LYAYNIMKLG GFFTLLIMAA FLIPFWIRHN RDSELIRKE
//
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