ID   CYF_SYNEL               Reviewed;         311 AA.
AC   P0C8N4; Q9X9T1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
OS   Synechococcus elongatus.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=32046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10760604; DOI=10.1016/s0167-4781(00)00048-8;
RA   Schneider D., Altenfeld U., Thomas H., Schrader S., Muehlenhoff U.,
RA   Roegner M.;
RT   "Sequence of the two operons encoding the four core subunits of the
RT   cytochrome b6f complex from the thermophilic cyanobacterium Synechococcus
RT   elongatus.";
RL   Biochim. Biophys. Acta 1491:364-368(2000).
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC       {ECO:0000255|HAMAP-Rule:MF_00610}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00610};
CC       Note=Binds 1 heme group covalently. {ECO:0000255|HAMAP-Rule:MF_00610};
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and
CC       PetN. The complex functions as a dimer. {ECO:0000255|HAMAP-
CC       Rule:MF_00610}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00610}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00610}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000255|HAMAP-
CC       Rule:MF_00610}.
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DR   EMBL; AJ243535; CAB46650.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C8N4; -.
DR   SMR; P0C8N4; -.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 2.60.40.830; -; 1.
DR   HAMAP; MF_00610; Cytb6_f_cytF; 1.
DR   InterPro; IPR024058; Cyt-f_TM.
DR   InterPro; IPR002325; Cyt_f.
DR   InterPro; IPR024094; Cyt_f_lg_dom.
DR   InterPro; IPR036826; Cyt_f_lg_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01333; Apocytochr_F_C; 1.
DR   Pfam; PF16639; Apocytochr_F_N; 1.
DR   PRINTS; PR00610; CYTOCHROMEF.
DR   SUPFAM; SSF103431; SSF103431; 1.
DR   SUPFAM; SSF49441; SSF49441; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   PROSITE; PS51010; CYTF; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Signal; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           28..311
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023846"
FT   TRANSMEM        279..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         28
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:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         48
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         51
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         52
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:0000255|HAMAP-Rule:MF_00610"
SQ   SEQUENCE   311 AA;  33340 MW;  CE433639665A11E9 CRC64;
     MKHFFKSLTL AIALAASVLF WSPQAQAYPF YAQQGYESPR EATGRIVCAN CHLAAKPIQV
     EVPQAVTPDS VFEAVVKIPY DTSVQQVLGD GSKGGLNVGA VLMLPEGFKI APPDRLPEEL
     QAKTSGIYYQ PYSDDQQNII LVGPLPGEQY QEIVFPILAP NPGTDKSIHF GKYAVHAGGN
     RGRGQVYPNG EKSNNNVFTA PIAGTITSIT PNPDGSTAVV ITPENGEAVT ETVPAGPELI
     VREGQTVVAG AALTNNPNVG GFGQKDTEIV LQDPNRIKWL LVFFAAITLS QILLVLKKKQ
     VEKVQAAEMS F