ID   CY551_HALHA             Reviewed;          78 AA.
AC   P00122;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cytochrome c-551;
DE   AltName: Full=Cytochrome c551;
OS   Halorhodospira halophila (Ectothiorhodospira halophila).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=1053;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=BN9626;
RX   PubMed=8215425; DOI=10.1006/abbi.1993.1484;
RA   Ambler R.P., Meyer T.E., Kamen M.D.;
RT   "Amino acid sequences of cytochromes c-551 from the halophilic purple
RT   phototrophic bacteria, Ectothiorhodospira halophila and E. halochloris.";
RL   Arch. Biochem. Biophys. 306:83-93(1993).
RN   [2]
RP   STRUCTURE BY NMR.
RC   STRAIN=BN9626;
RX   PubMed=8969306; DOI=10.1006/jmbi.1996.0662;
RA   Bersch B., Blackledge M.J., Meyer T.E., Marion D.;
RT   "Ectothiorhodospira halophila ferrocytochrome c551: solution structure and
RT   comparison with bacterial cytochromes c.";
RL   J. Mol. Biol. 264:567-584(1996).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is about +58 mV.;
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
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DR   PIR; S38755; CCER51.
DR   PDB; 1GKS; NMR; -; A=1-78.
DR   PDBsum; 1GKS; -.
DR   AlphaFoldDB; P00122; -.
DR   SMR; P00122; -.
DR   EvolutionaryTrace; P00122; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002323; Cyt_CIE.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00607; CYTCHROMECIE.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Transport.
FT   CHAIN           1..78
FT                   /note="Cytochrome c-551"
FT                   /id="PRO_0000108392"
FT   BINDING         14
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         17
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
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         55
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   HELIX           2..7
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   STRAND          9..12
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   HELIX           15..18
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   HELIX           31..35
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:1GKS"
FT   HELIX           64..75
FT                   /evidence="ECO:0007829|PDB:1GKS"
SQ   SEQUENCE   78 AA;  8258 MW;  C1AF8F3B5804509B CRC64;
     DGESIYINGT APTCSSCHDR GVAGAPELNA PEDWADRPSS VDELVESTLA GKGAMPAYDG
     RADREDLVKA IEYMLSTL