CYB_SULAC
ID CYB_SULAC Reviewed; 563 AA.
AC P39480; Q4J750;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cytochrome b;
GN Name=soxC; OrderedLocusNames=Saci_2087;
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=1372250; DOI=10.1002/j.1460-2075.1992.tb05117.x;
RA Luebben M., Kolmerer B., Saraste M.;
RT "An archaebacterial terminal oxidase combines core structures of two
RT mitochondrial respiratory complexes.";
RL EMBO J. 11:805-812(1992).
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: Binds 2 heme groups (b586 and b606) which are not covalently
CC bound to the protein.
CC -!- SUBUNIT: It is a component of at least 2 distinct terminal oxidases,
CC the quinol oxidase (SoxABC) and the alternate quinol oxidase with the
CC core components SoxM and a Rieske Fe-S protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY81381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X62643; CAA44511.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY81381.1; ALT_INIT; Genomic_DNA.
DR PIR; S21043; S21043.
DR RefSeq; WP_015385765.1; NC_007181.1.
DR AlphaFoldDB; P39480; -.
DR SMR; P39480; -.
DR STRING; 330779.Saci_2087; -.
DR TCDB; 3.D.4.1.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR EnsemblBacteria; AAY81381; AAY81381; Saci_2087.
DR GeneID; 3472600; -.
DR KEGG; sai:Saci_2087; -.
DR PATRIC; fig|330779.12.peg.2089; -.
DR eggNOG; arCOG01721; Archaea.
DR HOGENOM; CLU_038033_0_0_2; -.
DR BioCyc; MetaCyc:MON-21019; -.
DR BRENDA; 7.1.1.4; 6160.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF13631; Cytochrom_B_N_2; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..563
FT /note="Cytochrome b"
FT /id="PRO_0000061777"
FT TRANSMEM 36..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 101
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 198
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 212
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
SQ SEQUENCE 563 AA; 62787 MW; 17BE11274DF45A79 CRC64;
MLVEEKKSGI IDSILERLGI NEAPLFRTPD YMYNISYWLG AMVAASFAYT IITGLFLLLY
YQPAFAYQST QTIINSVPYG SVLLFSHLYG SYIMILLAYI HMFRNFYKGA YKKPRELQWV
TGVLLLALTL GASFFGYSLV SDVLGVNAID IGDQLLVGTG IPGATAIVGW LFGPGGSAAL
SSNPLVRSEL FDRLLGWHII MVFLLGVLFL FHFMLSERYG MTPATREKPK VPSYYTKEEQ
EKFNPWWPRN FVYMLSIVLI TWGIILFVPN LLANINGLPI VINPYPAPQA GSPQAVSVQP
YPPWFFLFLF KLVDFLLPNG IPITPILTIA LLVVGLVILM LLPFLDPSDS LYVTRRKFWT
WIMTTLAVYL VELSVWGYLE PGVPEPTSAQ IEFLGPPLVI IGIIVYLWPT ERKTKTVSTT
ATDSRVIKMN ITPMEILLGA VGTLSFAATL FNFIQFPTLI NGIILVPLGL FAIYALRRIS
FYVLGGKPVA SVGNTSSRIS LRKKIAFFGI IALFVVSLVL LGLMWTLPSV GPQATYAGMD
LGVILLLWGV AIQLYHYEIF VKE
