ID   CY1_ALLVD               Reviewed;         244 AA.
AC   O31216; D3RUZ3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cytochrome c1;
DE   Flags: Precursor;
GN   Name=petC; OrderedLocusNames=Alvin_0070;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   DOI=10.1023/A:1006052408216;
RA   Chen Y.L., Dincturk H.B., Qin H., Knaff D.B.;
RT   "The pet operon, encoding the prosthetic group-containing subunits of the
RT   cytochrome bc1 complex, of the purple sulfur bacterium Chromatium
RT   vinosum.";
RL   Photosyn. Res. 57:149-158(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
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; AF034104; AAB86975.1; -; Genomic_DNA.
DR   EMBL; CP001896; ADC61042.1; -; Genomic_DNA.
DR   RefSeq; WP_012969318.1; NC_013851.1.
DR   AlphaFoldDB; O31216; -.
DR   SMR; O31216; -.
DR   STRING; 572477.Alvin_0070; -.
DR   EnsemblBacteria; ADC61042; ADC61042; Alvin_0070.
DR   KEGG; alv:Alvin_0070; -.
DR   eggNOG; COG2857; Bacteria.
DR   HOGENOM; CLU_078597_0_0_6; -.
DR   OMA; MPHVLWE; -.
DR   OrthoDB; 1426747at2; -.
DR   Proteomes; UP000001441; 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: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   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Reference proteome; Respiratory chain; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..244
FT                   /note="Cytochrome c1"
FT                   /id="PRO_0000006559"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         50
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         53
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         54
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   244 AA;  27757 MW;  4376F7A1C1261FB3 CRC64;
     MRKLILATFL LLAPTALLAS GGGEHLESAN IDLRDQASLQ RGAKYFMNYC TGCHSLQYMR
     YNRLAKDLGI DEIALRQNLL FGDAKPGDLI TKAMTDDDAL KWFGVVPPDL TLVTRWRSPD
     WVYTYLKSFY LDDTRPYGVN NVLFPLVGMP HVLGDLQGRQ EAVMEPSHEP GGEPTIKGVK
     LVEEGGLSPQ EYDTMVRDIT NFLTYAGEPF QLERERIGRY VLLFLGFLFI LAYLLKKEYW
     KDVH