ID T0H967_9LEPT Unreviewed; 198 AA.
AC T0H967;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=SCO1/SenC {ECO:0000313|EMBL:EQA80358.1};
GN ORFNames=LEP1GSC193_4359 {ECO:0000313|EMBL:EQA80358.1};
OS Leptospira alstonii serovar Pingchang str. 80-412.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218564 {ECO:0000313|EMBL:EQA80358.1, ECO:0000313|Proteomes:UP000015445};
RN [1] {ECO:0000313|EMBL:EQA80358.1, ECO:0000313|Proteomes:UP000015445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=80-412 {ECO:0000313|EMBL:EQA80358.1,
RC ECO:0000313|Proteomes:UP000015445};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (MAY-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:EQA80358.1}.
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DR EMBL; AOHD02000040; EQA80358.1; -; Genomic_DNA.
DR RefSeq; WP_017808679.1; NZ_AOHD02000040.1.
DR AlphaFoldDB; T0H967; -.
DR STRING; 28452.A0128_07260; -.
DR Proteomes; UP000015445; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 73..77
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 198 AA; 22099 MW; 99FEDFD82C2180C7 CRC64;
MKERILFITV LFFGIGIGFF GWKGWKSESQ SGFEPIFVRE WSSSSLKNTD NLEIHLSEIP
GKLKLVYFGF SHCPDMCPRA LLDMSAAVRE LGDEGKNLTP IFISVDPERD SPELLAKYVK
QFPGERLIAL TGEKSRLDSL QSAFGAVSKK VSAPQLEGGY TVDHTVFLYV LDDRSRILVT
FPGGTDGKTL AKEIKKFL
//
