CY552_THETH
ID CY552_THETH Reviewed; 131 AA.
AC P04164;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytochrome c-552;
DE AltName: Full=Cytochrome c552;
DE Flags: Fragment;
GN Name=cycA;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).
RX PubMed=9281430; DOI=10.1006/jmbi.1997.1181;
RA Than M.E., Hof P., Huber R., Bourenkov G.P., Bartunik H.D., Buse G.,
RA Soulimane T.;
RT "Thermus thermophilus cytochrome-c552: a new highly thermostable
RT cytochrome-c structure obtained by MAD phasing.";
RL J. Mol. Biol. 271:629-644(1997).
CC -!- FUNCTION: This monoheme basic protein appears to function as an
CC electron donor to cytochrome oxidase in T.thermophilus.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1C52. {ECO:0000305}.
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DR PIR; A00112; CCTW5T.
DR PDB; 1C52; X-ray; 1.28 A; A=1-131.
DR PDB; 1QYZ; X-ray; 1.40 A; A=1-131.
DR PDB; 1R0Q; X-ray; 1.61 A; A=1-131.
DR PDB; 2FWL; NMR; -; A=1-131.
DR PDB; 3VNW; X-ray; 1.97 A; A=3-131.
DR PDBsum; 1C52; -.
DR PDBsum; 1QYZ; -.
DR PDBsum; 1R0Q; -.
DR PDBsum; 2FWL; -.
DR PDBsum; 3VNW; -.
DR AlphaFoldDB; P04164; -.
DR SMR; P04164; -.
DR DrugBank; DB02949; 2-Acetyl-Protoporphyrin Ix.
DR DrugBank; DB03224; 2-Formyl-Protoporphryn Ix.
DR EvolutionaryTrace; P04164; -.
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 Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Metal-binding; Transport.
FT CHAIN <1..131
FT /note="Cytochrome c-552"
FT /id="PRO_0000108402"
FT BINDING 11
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 14
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 15
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 BINDING 69
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 NON_TER 1
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1C52"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:1C52"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2FWL"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1C52"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:1C52"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:1C52"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1C52"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1C52"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1C52"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1C52"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1R0Q"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:1C52"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:1C52"
SQ SEQUENCE 131 AA; 14173 MW; 2E7E405D8A89C3BF CRC64;
QADGAKIYAQ CAGCHQQNGQ GIPGAFPPLA GHVAEILAKE GGREYLILVL LYGLQGQIEV
KGMKYNGVMS SFAQLKDEEI AAVLNHIATA WGDAKKVKGF KPFTAEEVKK LRAKKLTPQQ
VLAERKKLGL K
