CY1_RHOCA
ID CY1_RHOCA Reviewed; 280 AA.
AC P0CY49; P07058; P08501;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Cytochrome c1;
DE Flags: Precursor;
GN Name=petC;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GA;
RX PubMed=3004982; DOI=10.1111/j.1432-1033.1986.tb09437.x;
RA Gabellini N., Sebald W.;
RT "Nucleotide sequence and transcription of the fbc operon from
RT Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid
RT sequences of the FeS protein, cytochrome b and cytochrome c1.";
RL Eur. J. Biochem. 154:569-579(1986).
RN [2]
RP SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3004982 ORIGINATES FROM RHODOBACTER
RP CAPSULATUS.
RX PubMed=2821272; DOI=10.1016/0022-2836(87)90324-x;
RA Davidson E., Daldal F.;
RT "fbc operon, encoding the Rieske Fe-S protein cytochrome b, and cytochrome
RT c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is
RT from Rhodopseudomonas capsulata.";
RL J. Mol. Biol. 195:25-29(1987).
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.
CC -!- CAUTION: The sequence reported in PubMed:3004982 was thought to
CC originate from R.sphaeroides but was later shown to be derived from
CC R.capsulatus. {ECO:0000305|PubMed:2821272}.
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DR EMBL; X03476; CAA27196.1; -; Genomic_DNA.
DR PIR; C25405; C25405.
DR PDB; 1ZRT; X-ray; 3.50 A; D/Q=22-280.
DR PDBsum; 1ZRT; -.
DR AlphaFoldDB; P0CY49; -.
DR SMR; P0CY49; -.
DR EvolutionaryTrace; P0CY49; -.
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..21
FT CHAIN 22..280
FT /note="Cytochrome c1"
FT /id="PRO_0000006561"
FT TRANSMEM 249..267
FT /note="Helical; Note=Anchors to the membrane"
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 58
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 59
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 205
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 STRAND 31..36
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1ZRT"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 224..239
FT /evidence="ECO:0007829|PDB:1ZRT"
FT HELIX 243..272
FT /evidence="ECO:0007829|PDB:1ZRT"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1ZRT"
SQ SEQUENCE 280 AA; 30383 MW; A2A54A357DC976E5 CRC64;
MKKLLISAVS ALVLGSGAAL ANSNVQDHAF SFEGIFGKFD QAQLRRGFQV YSEVCSTCHG
MKFVPIRTLS DDGGPQLDPT FVREYAAGLD TIIDKDSGEE RDRKETDMFP TRVGDGMGPD
LSVMAKARAG FSGPAGSGMN QLFKGIGGPE YIYRYVTGFP EENPACAPEG IDGYYYNEVF
QVGGVPDTCK DAAGIKTTHG SWAQMPPALF DDLVTYEDGT PATVDQMGQD VASFLMWAAE
PKLVARKQMG LVAVVMLGLL SVMLYLTNKR LWAPYKRQKA
