ID   CY1_BLAVI               Reviewed;         282 AA.
AC   P81379;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cytochrome c1;
DE   Flags: Precursor;
GN   Name=petC; Synonyms=fbcC;
OS   Blastochloris viridis (Rhodopseudomonas viridis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Blastochloridaceae; Blastochloris.
OX   NCBI_TaxID=1079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19567 / DSM 133 / F;
RX   PubMed=2560136; DOI=10.1007/bf00259618;
RA   Verbist J., Lang F., Gabellini N., Oesterhelt D.;
RT   "Cloning and sequencing of the fbcF, B and C genes encoding the cytochrome
RT   b/c1 complex from Rhodopseudomonas viridis.";
RL   Mol. Gen. Genet. 219:445-452(1989).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; JQ0347; JQ0347.
DR   AlphaFoldDB; P81379; -.
DR   SMR; P81379; -.
DR   STRING; 1079.BVIR_2483; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProt.
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   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Respiratory chain; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..282
FT                   /note="Cytochrome c1"
FT                   /id="PRO_0000006564"
FT   TRANSMEM        253..273
FT                   /note="Helical; Note=Anchors to the membrane"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         65
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         66
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   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"
SQ   SEQUENCE   282 AA;  31262 MW;  E97DDCBC3F6A7346 CRC64;
     MTIKLRFVAS LALVFGLAAA SVPAQASGGD TPHLQSWSFA GPFGQYDKAQ LRRGFQVFQN
     VCVSCHTLEN GGFRNLPSRA APNWPLDEVR QLAASWPVQV KDINDKGDPM QRAPKLPDRI
     PSQYANEAAA RIIHNGAVPP DLSVIAKART FQRGFPWWVT DIFTQYNENG VDYIVALLNG
     YEDPPERFKV PDGSFYNKYF PGHIIGMTPP IADGLVTYGD GTPETQLQYS KDVAAFLMWA
     AEPTLDVRKR IGWWVLGFLV IFTGLLVATK IVVWRPVKKG LA