ID   C554_CERSP              Reviewed;         133 AA.
AC   P0C0X7; Q53142;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Cytochrome c-554;
DE   AltName: Full=Cytochrome c554;
DE   AltName: Full=High-potential cytochrome c;
GN   Name=cycF;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   STRAIN=MRE;
RX   PubMed=2543295; DOI=10.1016/0003-9861(89)90293-2;
RA   Bartsch R.G., Ambler R.P., Meyer T.E., Cusanovich M.A.;
RT   "Effect of aerobic growth conditions on the soluble cytochrome content of
RT   the purple phototrophic bacterium Rhodobacter sphaeroides: induction of
RT   cytochrome c554.";
RL   Arch. Biochem. Biophys. 271:433-440(1989).
CC   -!- FUNCTION: Monoheme c-type cytochrome, that is particularly expressed
CC       when cells generate energy via aerobic respiration.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Binds 1 heme group per subunit.
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DR   AlphaFoldDB; P0C0X7; -.
DR   SMR; P0C0X7; -.
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:0005506; F:iron ion binding; IEA:InterPro.
DR   InterPro; IPR010980; Cyt_c/b562.
DR   InterPro; IPR002321; Cyt_c_II.
DR   InterPro; IPR012127; Cyt_c_prime.
DR   InterPro; IPR015984; Cyt_c_prime_subgr.
DR   Pfam; PF01322; Cytochrom_C_2; 1.
DR   PIRSF; PIRSF000027; Cytc_c_prime; 1.
DR   PRINTS; PR00608; CYTCHROMECII.
DR   SUPFAM; SSF47175; SSF47175; 1.
DR   PROSITE; PS51009; CYTCII; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Periplasm; Pyrrolidone carboxylic acid; Transport.
FT   CHAIN           1..133
FT                   /note="Cytochrome c-554"
FT                   /id="PRO_0000108406"
FT   BINDING         17
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:2543295"
SQ   SEQUENCE   133 AA;  14065 MW;  172F879ECA4E6DD7 CRC64;
     QDARQIERMI EGRHGLMTLM AYELGKLGGM AKEETPYDAE VAGDAASNLS ALASVLSPEL
     FPKGSAVGEA EDSEALPAIW EKPDDFAQKI SDMEEAAAKM QAAAGTDLAS LQGAMRDLGA
     GCGSCHETYR QKD