CY1_CERSP
ID CY1_CERSP Reviewed; 285 AA.
AC Q02760;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome c1;
DE Flags: Precursor;
GN Name=petC; Synonyms=fbcC;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2176595; DOI=10.1111/j.1432-1033.1990.tb15633.x;
RA Yun C.-H., Beci R., Crofts A.R., Kaplan S., Gennis R.B.;
RT "Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1
RT complex from Rhodobacter sphaeroides. Characterization of fbc deletion
RT mutants and complementation by a site-specific mutational variant.";
RL Eur. J. Biochem. 194:399-411(1990).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC c1 functions as an electron donor to cytochrome c.
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; X56157; CAA39625.1; -; Genomic_DNA.
DR PIR; S13870; S13870.
DR PDB; 2FYN; X-ray; 3.20 A; B/E/H/K/N/Q=23-285.
DR PDB; 2QJK; X-ray; 3.10 A; B/E/H/K/N/Q=23-278.
DR PDB; 2QJP; X-ray; 2.60 A; B/E/H/K=23-278.
DR PDB; 2QJY; X-ray; 2.40 A; B/E/H/K/N/Q=23-285.
DR PDB; 5KKZ; X-ray; 2.97 A; B/F/L/P=23-285.
DR PDB; 5KLI; X-ray; 3.00 A; B/F/L/P=23-285.
DR PDBsum; 2FYN; -.
DR PDBsum; 2QJK; -.
DR PDBsum; 2QJP; -.
DR PDBsum; 2QJY; -.
DR PDBsum; 5KKZ; -.
DR PDBsum; 5KLI; -.
DR AlphaFoldDB; Q02760; -.
DR SMR; Q02760; -.
DR DIP; DIP-61257N; -.
DR IntAct; Q02760; 2.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR DrugBank; DB08690; Ubiquinone Q2.
DR EvolutionaryTrace; Q02760; -.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR PANTHER; PTHR10266; PTHR10266; 2.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Respiratory chain; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..22
FT CHAIN 23..285
FT /note="Cytochrome c1"
FT /evidence="ECO:0000269|PubMed:2176595"
FT /id="PRO_0000006563"
FT TRANSMEM 251..269
FT /note="Helical; Note=Anchors to the membrane"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 61
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 62
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 207
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2QJY"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5KKZ"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:2QJY"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2FYN"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:2QJY"
FT HELIX 245..275
FT /evidence="ECO:0007829|PDB:2QJY"
SQ SEQUENCE 285 AA; 30604 MW; A7B1E78B305D8AEE CRC64;
MIRKLTLTAA TALALSGGAA MAAGGGHVED VPFSFEGPFG TFDQHQLQRG LQVYTEVCAA
CHGMKFVPIR SLSEPGGPEL PEDQVRAYAT QFTVTDEETG EDREGKPTDH FPHSALENAA
DLSLMAKARA GFHGPMGTGI SQLFNGIGGP EYIYSVLTGF PEEPPKCAEG HEPDGFYYNR
AFQNGSVPDT CKDANGVKTT AGSWIAMPPP LMDDLVEYAD GHDASVHAMA EDVSAFLMWA
AEPKLMARKQ AGFTAVMFLT VLSVLLYLTN KRLWAGVKGK KKTNV
