ID   CYSD_CHLTI              Reviewed;          87 AA.
AC   P20958;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cytochrome subunit of sulfide dehydrogenase;
DE   AltName: Full=FCSD;
DE            Short=FC;
DE   AltName: Full=Flavocytochrome c cytochrome subunit;
GN   Name=fccA;
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.
RC   STRAIN=DSM 249 / 6230 / Tassajara;
RX   PubMed=2161842; DOI=10.1016/s0021-9258(19)38741-1;
RA   van Beeumen J., van Bun S., Meyer T.E., Bartsch R.G., Cusanovich M.A.;
RT   "Complete amino acid sequence of the cytochrome subunit and amino-terminal
RT   sequence of the flavin subunit of flavocytochrome c (sulfide dehydrogenase)
RT   from Chlorobium thiosulfatophilum.";
RL   J. Biol. Chem. 265:9793-9799(1990).
CC   -!- FUNCTION: Monoheme cytochrome that function as the electron transport
CC       subunit of sulfide dehydrogenase.
CC   -!- SUBUNIT: Dimer of one cytochrome and one flavoprotein.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
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DR   PIR; A36437; A36437.
DR   AlphaFoldDB; P20958; -.
DR   SMR; P20958; -.
DR   GO; GO:0042597; C:periplasmic space; 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   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   Periplasm; Transport.
FT   CHAIN           1..87
FT                   /note="Cytochrome subunit of sulfide dehydrogenase"
FT                   /id="PRO_0000108418"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         21
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         22
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   87 AA;  9351 MW;  B67791CF18ADDC3A CRC64;
     APEQSKSIPR GEILSLSCAG CHGTDGKSES IIPTIYGRSA EYIESALLDF KSGARPSTVM
     GRHAKGYSDE EIHQIAEYFG SLSTMNN