ID CY1_RHOCB Reviewed; 279 AA.
AC D5ANZ4; P07058; P08501;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Cytochrome c1;
DE Flags: Precursor;
GN Name=petC; OrderedLocusNames=RCAP_rcc02770;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2821268; DOI=10.1016/0022-2836(87)90323-8;
RA Davidson E., Daldal F.;
RT "Primary structure of the bc1 complex of Rhodopseudomonas capsulata.
RT Nucleotide sequence of the pet operon encoding the Rieske cytochrome b, and
RT cytochrome c1 apoproteins.";
RL J. Mol. Biol. 195:13-24(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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; X05630; CAA29118.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE86499.1; -; Genomic_DNA.
DR PIR; C29336; C29336.
DR PDB; 6XI0; EM; 3.30 A; D/Q=1-279.
DR PDB; 6XKT; EM; 3.75 A; D/Q=1-279.
DR PDB; 6XKU; EM; 4.20 A; D/Q=1-279.
DR PDB; 6XKV; EM; 3.50 A; D/Q=1-279.
DR PDB; 6XKW; EM; 5.20 A; D/Q=1-279.
DR PDB; 6XKX; EM; 6.10 A; D/Q=1-279.
DR PDB; 6XKZ; EM; 7.20 A; D/Q=1-279.
DR PDBsum; 6XI0; -.
DR PDBsum; 6XKT; -.
DR PDBsum; 6XKU; -.
DR PDBsum; 6XKV; -.
DR PDBsum; 6XKW; -.
DR PDBsum; 6XKX; -.
DR PDBsum; 6XKZ; -.
DR AlphaFoldDB; D5ANZ4; -.
DR EMDB; EMD-22189; -.
DR EMDB; EMD-22224; -.
DR EMDB; EMD-22225; -.
DR EMDB; EMD-22226; -.
DR EMDB; EMD-22227; -.
DR EMDB; EMD-22228; -.
DR EMDB; EMD-22230; -.
DR SMR; D5ANZ4; -.
DR STRING; 272942.RCAP_rcc02770; -.
DR TCDB; 3.D.3.1.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR KEGG; rcp:RCAP_rcc02770; -.
DR eggNOG; COG2857; Bacteria.
DR HOGENOM; CLU_040334_1_2_5; -.
DR OrthoDB; 9808471at2; -.
DR Proteomes; UP000002361; Chromosome.
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; Cytochrome c-like domain; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR PANTHER; PTHR10266; CYTOCHROME C1; 1.
DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; Cytochrome c; 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; Reference proteome; Respiratory chain; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..279
FT /note="Cytochrome c1"
FT /id="PRO_0000409866"
FT TRANSMEM 248..266
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 58
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 204
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..35
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 242..270
FT /evidence="ECO:0007829|PDB:6XI0"
SQ SEQUENCE 279 AA; 30322 MW; 5B26E163B7D52DBD CRC64;
MKKLLISAVS ALVLGSGAAF ANSNVPDHAF SFEGIFGKYD QAQLRRGFQV YNEVCSACHG
MKFVPIRTLA DDGGPQLDPT FVREYAAGLD TIIDKDSGEE RDRKETDMFP TRVGDGMGPD
LSVMAKARAG FSGPAGSGMN QLFKGMGGPE YIYNYVIGFE ENPECAPEGI DGYYYNKTFQ
IGGVPDTCKD AAGVKITHGS WARMPPPLVD DQVTYEDGTP ATVDQMAQDV SAFLMWAAEP
KLVARKQMGL VAMVMLGLLS VMLYLTNKRL WAPYKGHKA
//
