CBSA_SULAC
ID CBSA_SULAC Reviewed; 462 AA.
AC O54088; Q4J7R7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Cytochrome b558/566 subunit A;
GN Name=cbsA; OrderedLocusNames=Saci_1858;
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], PARTIAL PROTEIN SEQUENCE, AND MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=9575144; DOI=10.1074/jbc.273.20.12032;
RA Hettmann T., Schmidt C.L., Anemueller S., Zaehringer U., Moll H.,
RA Petersen A., Schaefer G.;
RT "Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius. A novel
RT highly glycosylated, membrane-bound b-type hemoprotein.";
RL J. Biol. Chem. 273:12032-12040(1998).
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).
RN [3]
RP GLYCOSYLATION AT ASN-144 AND ASN-164, AND STRUCTURE OF CARBOHYDRATE.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=10866817; DOI=10.1046/j.1432-1327.2000.01446.x;
RA Zaehringer U., Moll H., Hettmann T., Knirel Y.A., Schaefer G.;
RT "Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a
RT unique Asn-linked highly branched hexasaccharide chain containing 6-
RT sulfoquinovose.";
RL Eur. J. Biochem. 267:4144-4149(2000).
CC -!- FUNCTION: Monoheme cytochrome whose physiological function is not yet
CC clear.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is >350 mV.;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: N-glycosylated on at least seven Asn residues by identical
CC hexasaccharide units composed of Man, GlcNAc, Glc and 6-deoxy-6-
CC sulfoglucose residues in the molar ration of 2:2:1:1.
CC {ECO:0000269|PubMed:10866817}.
CC -!- PTM: O-glycosylated on probably as many as 35 positions by single Man
CC residues. {ECO:0000269|PubMed:10866817}.
CC -!- MASS SPECTROMETRY: Mass=64210; Method=MALDI; Note=Glycosylated.;
CC Evidence={ECO:0000269|PubMed:9575144};
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DR EMBL; Y10108; CAA71195.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY81164.1; -; Genomic_DNA.
DR RefSeq; WP_011278666.1; NC_007181.1.
DR AlphaFoldDB; O54088; -.
DR STRING; 330779.Saci_1858; -.
DR GlyConnect; 119; 1 N-Linked glycan.
DR iPTMnet; O54088; -.
DR EnsemblBacteria; AAY81164; AAY81164; Saci_1858.
DR GeneID; 3474781; -.
DR KEGG; sai:Saci_1858; -.
DR PATRIC; fig|330779.12.peg.1806; -.
DR eggNOG; arCOG06015; Archaea.
DR HOGENOM; CLU_575729_0_0_2; -.
DR OMA; MYEVDTA; -.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR InterPro; IPR019020; Cyt-c552/DMSO_Rdtase_haem-bd.
DR InterPro; IPR017572; Cyt_b558/566_suA.
DR Pfam; PF09459; EB_dh; 1.
DR SMART; SM00887; EB_dh; 1.
DR TIGRFAMs; TIGR03154; sulfolob_CbsA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Glycoprotein;
KW Heme; Iron; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..462
FT /note="Cytochrome b558/566 subunit A"
FT /id="PRO_0000089383"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..456
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10866817"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10866817"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 50730 MW; 74D93935B09D5E72 CRC64;
MSLKIKSKIT IGVLLIIFLL SIIFTLENVS LAQTSPQISV YKVVGSADLS NPGSAGYWSQ
IPWTNISLTA NIPMAPTSGL THYLLVKAAW NGSWIFILEE WQAPEPAFNA WSTAVAGIYP
NASGPGLFRM IELTPGTTYS LERNYTNYVS IINGKEETGR IVFNYSGITL PAPNNTEITV
MSNGTILLWH SPRPVEDLLY NDGMFYGYYV NSTWYYPDRA AIMWYLGSGV PTKDDMNIGG
KYPGQQFDGI TFKDAGGSLA QSGGSANIWM WVSGATWNNS TYDPAFKSNI WQNESLTGLS
YVDSGNHGFA VPLYTNNTNM YEVDTAGIWY TPVASEGLNG SLFFIWTGAK YENGSWVVEF
ARPLSVPLDY QPFMPNITVG KTYYVAFAVW QGRLGETLFD KSITSSFLSL ELVTTPPTST
TTSTSPVTTI SSAIPPVTLY VTIIGVVVAL VALVILYVVF RR
