ID   C555_CHLTI              Reviewed;          86 AA.
AC   P00123;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Cytochrome c-555;
DE   AltName: Full=Cytochrome c555;
OS   Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp.
OS   thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=115852;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=188412; DOI=10.1042/bj1590757;
RA   van Beeumen J., Ambler R.P., Meyer T.E., Kamen M.D., Olson J.M., Shaw E.K.;
RT   "The amino acid sequences of the cytochromes c-555 from two green sulphur
RT   bacteria of the genus Chlorobium.";
RL   Biochem. J. 159:757-769(1976).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=202947; DOI=10.1073/pnas.74.12.5244;
RA   Korszun Z.R., Salemme F.R.;
RT   "Structure of cytochrome c555 of Chlorobium thiosulfatophilum: primitive
RT   low-potential cytochrome c.";
RL   Proc. Natl. Acad. Sci. U.S.A. 74:5244-5247(1977).
CC   -!- FUNCTION: This basic c-type monoheme cytochrome has been found
CC       exclusively in the green photosynthetic bacteria, although its role in
CC       bacterial photosynthesis is not established. It has an unusually low
CC       redox potential compared with mitochondrial cytochrome c. It is
CC       reactive with cytochrome c oxidases but not with reductases.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
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DR   AlphaFoldDB; P00123; -.
DR   SMR; P00123; -.
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   GO; GO:0015979; P:photosynthesis; 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; IPR002323; Cyt_CIE.
DR   PANTHER; PTHR40942; PTHR40942; 1.
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   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Photosynthesis; Transport.
FT   CHAIN           1..86
FT                   /note="Cytochrome c-555"
FT                   /id="PRO_0000108408"
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         60
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"
SQ   SEQUENCE   86 AA;  8780 MW;  0882D21350DB9D4E CRC64;
     YDAAAGKATY DASCAMCHKT GMMGAPKVGD KAAWAPHIAK GMNVMVANSI KGYKGTKGMM
     PAKGGNPKLT DAQVGNAVAY MVGQSK