ID   SOXE_SULAC              Reviewed;         199 AA.
AC   Q53765; Q4J6N4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Sulfocyanin;
DE   AltName: Full=Blue copper protein;
GN   Name=soxE; OrderedLocusNames=Saci_2262;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=7608970; DOI=10.1006/jmbi.1995.0371;
RA   Castresana J., Luebben M., Saraste M.;
RT   "New archaebacterial genes coding for redox proteins: implications for the
RT   evolution of aerobic metabolism.";
RL   J. Mol. Biol. 250:202-210(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: The 4 redox proteins SoxE, SoxF, SoxG and SoxH probably form
CC       part of a membrane respiratory complex together with SoxM, a catalytic
CC       subunit of cytochrome oxidase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY81548.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z48338; CAA88317.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY81548.1; ALT_INIT; Genomic_DNA.
DR   PIR; S56155; S56155.
DR   RefSeq; WP_015385793.1; NC_007181.1.
DR   AlphaFoldDB; Q53765; -.
DR   SMR; Q53765; -.
DR   STRING; 330779.Saci_2262; -.
DR   EnsemblBacteria; AAY81548; AAY81548; Saci_2262.
DR   GeneID; 3474523; -.
DR   KEGG; sai:Saci_2262; -.
DR   PATRIC; fig|330779.12.peg.2271; -.
DR   eggNOG; arCOG03700; Archaea.
DR   HOGENOM; CLU_105306_1_0_2; -.
DR   BioCyc; MetaCyc:MON-21011; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR010532; SoxE.
DR   PIRSF; PIRSF022145; Sulfocyanin; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR03094; sulfo_cyanin; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Copper; Electron transport; Membrane; Metal-binding;
KW   Reference proteome; Respiratory chain; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..199
FT                   /note="Sulfocyanin"
FT                   /id="PRO_0000085587"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          79..188
FT                   /note="Plastocyanin-like"
FT   BINDING         110
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   199 AA;  20404 MW;  A49A7570AFF98BB0 CRC64;
     MKAQSSVLPV VVGILVVIIA VAVGVYVYNQ YVMLSSPSAS SSTGTSTGPS KISIPYSSSN
     KTVFLTIVVE SSSNVNQFNF NGTSSGSLVI YIPAGSTVIV KFINQESLPH NLVLLQNSTP
     TPQSPEISSD GKIIDIVGAT TSNYDVNGIS GGASAEGVWG PISAGDYMLV CGILGHAASG
     MWAVLVASNN VTAPYAVID