ID   CY1_RHORU               Reviewed;         272 AA.
AC   P23135;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cytochrome c1;
DE   Flags: Precursor;
GN   Name=petC;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-50.
RC   STRAIN=FR1;
RX   PubMed=2176269; DOI=10.1007/bf00262431;
RA   Majewski C., Trebst A.;
RT   "The pet genes of Rhodospirillum rubrum: cloning and sequencing of the
RT   genes for the cytochrome bc1-complex.";
RL   Mol. Gen. Genet. 224:373-382(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   -!- 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; X55387; CAA39060.1; -; Genomic_DNA.
DR   PIR; S12258; CCQF1R.
DR   AlphaFoldDB; P23135; -.
DR   SMR; P23135; -.
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; 1.
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   Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Respiratory chain; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:2176269"
FT   CHAIN           25..272
FT                   /note="Cytochrome c1"
FT                   /evidence="ECO:0000269|PubMed:2176269"
FT                   /id="PRO_0000006562"
FT   TRANSMEM        244..261
FT                   /note="Helical; Note=Anchors to the membrane"
FT                   /evidence="ECO:0000255"
FT   BINDING         61
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         64
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                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         200
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   272 AA;  29495 MW;  D2575CEBE7CC9332 CRC64;
     MTTIVKRALV AAGMVLAIGG AAQANEGGVS LHKQDWSWKG IFGRYDQPQL QRGFQVFHEV
     CSTCHGMKRV AYRNLSALGF SEDGIKELAA EKEFPAGPDD NGDMFTRPGT PADHIPSPFA
     NDKAAAAANG GAAPPDLSLL AKARPGGPNY IYSLLEGYAS DSPGEPAEWW VKQQQEKGLE
     VAFNEAKYFN DYFPGHAISM PPPLMDDLIT YEDGTAATKD QMAQDVVAYL NWAAEPELDA
     RKSLGLKVLL FLGVLTAMLL ALKLAIWRDV KH