CBSA_SACS2
ID CBSA_SACS2 Reviewed; 479 AA.
AC P58029;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cytochrome b558/566 subunit A;
GN Name=cbsA; OrderedLocusNames=SSO2801; ORFNames=C48_011;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC -!- FUNCTION: Monoheme cytochrome whose physiological function is not yet
CC clear. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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DR EMBL; AE006641; AAK42914.1; -; Genomic_DNA.
DR PIR; C90457; C90457.
DR AlphaFoldDB; P58029; -.
DR STRING; 273057.SSO2801; -.
DR EnsemblBacteria; AAK42914; AAK42914; SSO2801.
DR KEGG; sso:SSO2801; -.
DR PATRIC; fig|273057.12.peg.2887; -.
DR eggNOG; arCOG06015; Archaea.
DR HOGENOM; CLU_575729_0_0_2; -.
DR OMA; MYEVDTA; -.
DR Proteomes; UP000001974; 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 3: Inferred from homology;
KW Cell membrane; Electron transport; Glycoprotein; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..479
FT /note="Cytochrome b558/566 subunit A"
FT /id="PRO_0000089384"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 52532 MW; 7C92B0B91A8245B4 CRC64;
MLKPFCEKMS IKRKSKYTLG VLLLASFLAI IMGLANVPMA QTSPQIPVYK VVGNADLSNP
GSASYWSQIP WINISLTANI PMAPTSGLTH YLLVKAVWNG SWIIILERWY APEPAFGAWS
AAAAALYPPA SGPGLFRQIM LTPGTTYTIE KNYTNYFSIV NGNIIQGRLV LNYSGILLPA
PNDTQITVLS NGTIILWHSP RPIEDLLYSD GMFYGYYTNN TWYYPDRAAI MWYMGSVIPP
TKDGMNIGGK VPGQAFDGVT FNDTGGSLVQ PGGAANIWMW VSGATWNNAT YDPAFKVNLW
QNTSLTGLPY IDPDNHGFAV PLYTNNTNMY EVDTAGIWYT PVTTSGLNGS LFFIWTGATY
QNGYWTVEFA RPLAVPSAYA KWMPNITVGK TYYVAFAVWQ GKLGETLFDK SITSNFLTLE
LVTTPPTSTT TSTISSTSVT TTTSITTVTS IPSTTIYVTI VGVVIAIIAL IILYVVFRR