ID   C555_CHLTE              Reviewed;         108 AA.
AC   Q8KG93;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cytochrome c-555;
DE   AltName: Full=Cytochrome c555;
DE   Flags: Precursor;
GN   OrderedLocusNames=CT0075;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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   EMBL; AE006470; AAM71323.1; -; Genomic_DNA.
DR   RefSeq; NP_660981.1; NC_002932.3.
DR   RefSeq; WP_010931769.1; NC_002932.3.
DR   PDB; 4J20; X-ray; 1.30 A; A/B=21-108.
DR   PDBsum; 4J20; -.
DR   AlphaFoldDB; Q8KG93; -.
DR   SMR; Q8KG93; -.
DR   STRING; 194439.CT0075; -.
DR   EnsemblBacteria; AAM71323; AAM71323; CT0075.
DR   KEGG; cte:CT0075; -.
DR   eggNOG; COG3245; Bacteria.
DR   HOGENOM; CLU_082349_4_1_10; -.
DR   OMA; KACQVCH; -.
DR   OrthoDB; 1469969at2; -.
DR   Proteomes; UP000001007; Chromosome.
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   3D-structure; Electron transport; Heme; Iron; Metal-binding;
KW   Photosynthesis; Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..108
FT                   /note="Cytochrome c-555"
FT                   /id="PRO_0000006545"
FT   BINDING         36
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         39
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         40
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         82
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           25..35
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   HELIX           53..60
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   HELIX           64..73
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:4J20"
FT   HELIX           93..105
FT                   /evidence="ECO:0007829|PDB:4J20"
SQ   SEQUENCE   108 AA;  10892 MW;  9711CB0A43B8825C CRC64;
     MSRFVSAALV GAALLVSGNA FAYDAAAGKA TYDASCATCH KTGMMGAPKV GDKAAWAPRI
     AQGMNTLVSK SIKGYKGTKG MMPAKGGNAK LTDAQVGNAV AYMVGQSK