ID W0F253_9BACT Unreviewed; 274 AA.
AC W0F253;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Electron transporter SenC {ECO:0000313|EMBL:AHF15878.1};
GN ORFNames=NIASO_13355 {ECO:0000313|EMBL:AHF15878.1};
OS Niabella soli DSM 19437.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF15878.1, ECO:0000313|Proteomes:UP000003586};
RN [1] {ECO:0000313|EMBL:AHF15878.1, ECO:0000313|Proteomes:UP000003586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CP007035; AHF15878.1; -; Genomic_DNA.
DR RefSeq; WP_025298930.1; NZ_CP007035.1.
DR AlphaFoldDB; W0F253; -.
DR STRING; 929713.NIASO_13355; -.
DR KEGG; nso:NIASO_13355; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_2_0_10; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000003586; 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; SCO1 PROTEIN HOMOLOG; 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:UP000003586};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..227
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 189
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 92..96
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 274 AA; 31119 MW; 0DCA4C1B63A7C21F CRC64;
MNKTAIYGIL LAIILPVACY FIVDHYSKTA VILPPRFFPD SINSRLKDGK KVSDTIWHQL
SNFKLTNQMG DTVTLDKYRG KTIIADFFFT HCPTICPRLT MNMRRLQQSV TNLQRVGDRM
NKDVQFLSFS IDPERDSVPQ LKAWADRFQV DPDQWDLLTG DKKTIYDLAL NDMKIGLVDG
KGIDTSFIHT DHFVLIDSSR VIRGFYHGLD SASLAKLSQD LILLTLEKKP NEKGPLSGQM
NFLAAVFLFA ALLIGLFLIV FKKKQNVNSV LDQE
//
