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Database: UniProt
Entry: F6GIU3_LACS5
LinkDB: F6GIU3_LACS5
Original site: F6GIU3_LACS5 
ID   F6GIU3_LACS5            Unreviewed;       251 AA.
AC   F6GIU3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:AEH01236.1};
GN   OrderedLocusNames=Lacal_1388 {ECO:0000313|EMBL:AEH01236.1};
OS   Lacinutrix sp. (strain 5H-3-7-4).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lacinutrix.
OX   NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH01236.1, ECO:0000313|Proteomes:UP000008297};
RN   [1] {ECO:0000313|EMBL:AEH01236.1, ECO:0000313|Proteomes:UP000008297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH01236.1,
RC   ECO:0000313|Proteomes:UP000008297};
RX   PubMed=21725025; DOI=10.1128/JB.05518-11;
RA   Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA   Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA   Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA   Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT   "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT   Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT   family Flavobacteriaceae.";
RL   J. Bacteriol. 193:4545-4546(2011).
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; CP002825; AEH01236.1; -; Genomic_DNA.
DR   RefSeq; WP_013870015.1; NC_015638.1.
DR   AlphaFoldDB; F6GIU3; -.
DR   STRING; 983544.Lacal_1388; -.
DR   KEGG; lan:Lacal_1388; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_2_0_10; -.
DR   OMA; YVVEFFF; -.
DR   OrthoDB; 9811998at2; -.
DR   Proteomes; UP000008297; Chromosome.
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   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR   PANTHER; PTHR12151:SF25; LDI DOMAIN-CONTAINING PROTEIN; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..228
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         103
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         107
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         192
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        103..107
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   251 AA;  28445 MW;  32359C4301E98291 CRC64;
     MKKKNYSYIG IAFIILVFGI IFIPRIVNRI KDNKIVDNNK SRSVGIANPS DEEKKALALS
     FIEINGKPKK VPNFSFTNQD GETITQDDYL GKVYVVEFFF TTCPTICPRM NRNLIEIQNA
     FKNEDGFGIA SFSIMPEVDT PEVLKAYAQD YGVTNPNWNL MTGEEKAIFD LANIGFNIFV
     GKVADDEMGF EHSGDFALID KNGFIRSRKD AFGNPKIFYK GVISEQEKMD EDGNEQEISM
     LKEDIKKLLN E
//
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