ID   CY551_BACP3             Reviewed;         111 AA.
AC   Q56247;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome c-551;
DE   AltName: Full=Cytochrome c551;
DE   Flags: Precursor;
GN   Name=cccA;
OS   Bacillus sp. (strain PS3).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-67; 75-82 AND
RP   91-111, AND MASS SPECTROMETRY.
RX   PubMed=7916623; DOI=10.1016/0005-2728(93)90175-f;
RA   Fujiwara Y., Oka M., Hamamoto T., Sone N.;
RT   "Cytochrome c-551 of the thermophilic bacterium PS3, DNA sequence and
RT   analysis of the mature cytochrome.";
RL   Biochim. Biophys. Acta 1144:213-219(1993).
CC   -!- FUNCTION: Appears to mediate electron flow from the cytochrome b6f
CC       complex to an alternative terminal oxidase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MASS SPECTROMETRY: Mass=10509.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7916623};
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DR   EMBL; X63125; CAA44835.1; -; Genomic_DNA.
DR   PIR; S43726; S43726.
DR   AlphaFoldDB; Q56247; -.
DR   SMR; Q56247; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; 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: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; IPR012218; Cyt_c_BACSU-c550-rel.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PIRSF; PIRSF000025; Cytc_Bsub_c550; 1.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Lipoprotein; Membrane; Metal-binding; Palmitate; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000305"
FT   CHAIN           19..111
FT                   /note="Cytochrome c-551"
FT                   /id="PRO_0000006529"
FT   BINDING         51
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         54
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
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   BINDING         90
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   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  11136 MW;  B4AA17DA6504C985 CRC64;
     MKWKLAAMFL GVSLALAACG GGGDNAGEKN GGSNGGGDTA AAAEQIFKQN CASCHGQDLS
     GGVGPNLQKV GSKYSKDEIK NIIANGRGAM PAGIIKGEDA DKVAEWLAAK K