CY552_PARDE
ID CY552_PARDE Reviewed; 176 AA.
AC P54820;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cytochrome c-552;
DE AltName: Full=Cytochrome c552;
GN Name=cycM;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 66-76; 132-139
RP AND 164-175.
RC STRAIN=Pd 1235;
RX PubMed=7628479; DOI=10.1111/j.1432-1033.1995.tb20695.x;
RA Turba A., Jetzek M., Ludwig B.;
RT "Purification of Paracoccus denitrificans cytochrome c552 and sequence
RT analysis of the gene.";
RL Eur. J. Biochem. 231:259-265(1995).
CC -!- FUNCTION: Mediates the electron transport between the cytochrome bc1
CC complex and cytochrome-c oxidase.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; X70367; CAA49830.1; -; Genomic_DNA.
DR PIR; S65941; S31922.
DR PDB; 1C7M; NMR; -; A=78-176.
DR PDB; 1I6D; NMR; -; A=78-176.
DR PDB; 1I6E; NMR; -; A=78-176.
DR PDB; 1QL3; X-ray; 1.40 A; A/B/C/D=78-176.
DR PDB; 1QL4; X-ray; 1.50 A; A/B/C/D=78-176.
DR PDB; 3M97; X-ray; 1.33 A; X=38-176.
DR PDBsum; 1C7M; -.
DR PDBsum; 1I6D; -.
DR PDBsum; 1I6E; -.
DR PDBsum; 1QL3; -.
DR PDBsum; 1QL4; -.
DR PDBsum; 3M97; -.
DR AlphaFoldDB; P54820; -.
DR BMRB; P54820; -.
DR SMR; P54820; -.
DR DrugBank; DB03317; Ferroheme C.
DR EvolutionaryTrace; P54820; -.
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: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; IPR002327; Cyt_c_1A/1B.
DR PANTHER; PTHR11961; PTHR11961; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..176
FT /note="Cytochrome c-552"
FT /id="PRO_0000108401"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT BINDING 90
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 94
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 126
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 154
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 HELIX 71..76
FT /evidence="ECO:0007829|PDB:3M97"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:3M97"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3M97"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3M97"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3M97"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3M97"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:3M97"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:3M97"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3M97"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:3M97"
SQ SEQUENCE 176 AA; 18209 MW; 99FE93503FBC2855 CRC64;
MFDTMTVTKA AGALIGSLLF LLLMSWAASG IFHVGTSGHG AEGEEHAQAY TYPVESAGGA
EGEAVDEGPD FATVLASADP AAGEKVFGKC KACHKLDGND GVGPHLNGVV GRTVAGVDGF
NYSDPMKAHG GDWTPEALQE FLTNPKAVVK GTKMAFAGLP KIEDRANLIA YLEGQQ