ID   CYF_OSTTA               Reviewed;         307 AA.
AC   Q0P3K3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610}; OrderedLocusNames=OtCpg00490;
OS   Ostreococcus tauri.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595;
RX   PubMed=17251180; DOI=10.1093/molbev/msm012;
RA   Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.;
RT   "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus
RT   tauri: organelle genomes of the smallest eukaryote are examples of
RT   compaction.";
RL   Mol. Biol. Evol. 24:956-968(2007).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00610}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00610}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000255|HAMAP-
CC       Rule:MF_00610}.
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DR   EMBL; CR954199; CAL36374.1; -; Genomic_DNA.
DR   RefSeq; YP_717252.1; NC_008289.1.
DR   AlphaFoldDB; Q0P3K3; -.
DR   SMR; Q0P3K3; -.
DR   STRING; 70448.Q0P3K3; -.
DR   PRIDE; Q0P3K3; -.
DR   GeneID; 4238837; -.
DR   KEGG; ota:OstapCp49; -.
DR   eggNOG; ENOG502QPT8; Eukaryota.
DR   InParanoid; Q0P3K3; -.
DR   OrthoDB; 826802at2759; -.
DR   Proteomes; UP000009170; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
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   Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Plastid; Reference proteome; Signal; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           25..307
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000275435"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         25
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         45
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
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         49
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   307 AA;  32963 MW;  F130A6EE725F8905 CRC64;
     MKKNLFLVSV FASLFVGTAN NALAYPMYAQ QGYENPREAT GRIVCANCHL AQKPVDIEVP
     QAVLPDSVFE AVVKIPYNQE VKQVLGNGKK GGLNVGAVLI LPDGFTMAPA DRMSAELKEK
     VGKLYFQPYS EDKQNILIVG PVPGKKYSEM TFPLLSPDPA TNKKVNYLTY PIYLGGNRGR
     GQVYPDGSKS NNTVYNAAAA GKIAAINPTE KGTDVVIDKV DGGSVTVAIP SGPDLLVSVG
     DTVAADQPIT NNPNVGGFGQ GETEIVLQNP ARLQGLVIFL GFVLIAQVFL VLKKKQFEKV
     QLSEMNF