ID S7VSC4_9FLAO Unreviewed; 226 AA.
AC S7VSC4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=SCO1/SenC family lipoprotein {ECO:0000313|EMBL:EPR72242.1};
GN ORFNames=ADIWIN_2742 {ECO:0000313|EMBL:EPR72242.1};
OS Winogradskyella psychrotolerans RS-3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR72242.1, ECO:0000313|Proteomes:UP000014962};
RN [1] {ECO:0000313|EMBL:EPR72242.1, ECO:0000313|Proteomes:UP000014962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-3 {ECO:0000313|EMBL:EPR72242.1,
RC ECO:0000313|Proteomes:UP000014962};
RX PubMed=23950132;
RA Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT Ocean.";
RL Genome Announc. 1:e00630-e00613(2013).
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:EPR72242.1}.
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; ATMR01000126; EPR72242.1; -; Genomic_DNA.
DR RefSeq; WP_020895078.1; NZ_ATMR01000126.1.
DR AlphaFoldDB; S7VSC4; -.
DR STRING; 641526.ADIWIN_2742; -.
DR PATRIC; fig|641526.4.peg.2722; -.
DR eggNOG; COG1999; Bacteria.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000014962; 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 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 Lipoprotein {ECO:0000313|EMBL:EPR72242.1};
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:UP000014962};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..222
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 185
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 96..100
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 226 AA; 26083 MW; 861A00845EE7755C CRC64;
MSFLSFFKGY KNFGIFFSIL CVIIIAIIYN VLNVKHTLPI YQPGMVSEEL VDSTIQHQLK
YHKIADFSLT NQNGETITQD NYKDKIYVAD FFFTTCQTIC PIMTKNMEQI QKAIINDNDI
MLLSHSVTPK IDSVAQLKKY ALEKGVIDRK WNLVTGDKKQ IYELARKSYL AVKTDGNGDQ
FDMIHTENFM LIDKKRQIRG FYDGTNPEDI DQLLQDIETL KYFGGS
//
