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 27-MAR-2024, entry version 104.
DE RecName: Full=Cytochrome c-551;
DE AltName: Full=Cytochrome c551;
DE Flags: Precursor;
GN Name=cccA;
OS Bacillus sp. (strain PS3).
OC Bacteria; Bacillota; 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: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; Cytochrome c-like domain; 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 PANTHER; PTHR37823; CYTOCHROME C-553-LIKE; 1.
DR PANTHER; PTHR37823:SF4; MENAQUINOL-CYTOCHROME C REDUCTASE CYTOCHROME B_C SUBUNIT; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000025; Cytc_Bsub_c550; 1.
DR SUPFAM; SSF46626; Cytochrome c; 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
//
