ID W8VUY9_9FLAO Unreviewed; 224 AA.
AC W8VUY9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=SCO1/SenC family lipoprotein {ECO:0000313|EMBL:BAO54998.1};
GN ORFNames=NMS_0989 {ECO:0000313|EMBL:BAO54998.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO54998.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO54998.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO54998.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; AP014548; BAO54998.1; -; Genomic_DNA.
DR RefSeq; WP_041495677.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VUY9; -.
DR STRING; 1454201.NMS_0989; -.
DR HOGENOM; CLU_050131_2_0_10; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000031760; 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 Lipoprotein {ECO:0000313|EMBL:BAO54998.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..218
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 98
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 94..98
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 224 AA; 25965 MW; F486115F465A85FA CRC64;
MLKFIKDNKY RILFMVMLCA CIMAAFQYAL TPERKLAILQ PDQFDPSLVD DSMLFVKKYH
KIAPFSLVNQ NGDTITQADY EGKIYVADFF FTTCPSICPV MTKNMTLLQE EFKNDPEVML
LSHSVTPEID SVSVLREYAD RKGVMDSKWN LVTGDRQQIY DLARKSYLAV KKNKYGGENA
MIHTENFLLI DKEGRLRERS YDGTDEEEIE ALIEDIYVLK QSYK
//
