ID   CYF_CHLVU               Reviewed;         315 AA.
AC   P56316;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA;
OS   Chlorella vulgaris (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAM C-27 / Tamiya;
RX   PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA   Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA   Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA   Yoshinaga K., Sugiura M.;
RT   "Complete nucleotide sequence of the chloroplast genome from the green alga
RT   Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT   division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group covalently. {ECO:0000250};
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:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA57987.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB001684; BAA57987.1; ALT_FRAME; Genomic_DNA.
DR   PIR; T07339; T07339.
DR   RefSeq; NP_045911.2; NC_001865.1.
DR   AlphaFoldDB; P56316; -.
DR   SMR; P56316; -.
DR   PRIDE; P56316; -.
DR   GeneID; 809200; -.
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; Signal; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..315
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023811"
FT   TRANSMEM        281..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         31
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         51
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
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"
SQ   SEQUENCE   315 AA;  34213 MW;  843028C9F11133D2 CRC64;
     MRTFLKFSTL VSKGVLVLVC SFFLTASSNA YPIFAQQNYA NPREANGRIV CANCHLAEKP
     IEIEVPQAVL PDTVFEAVVK IPYDKQIKQV LANGKKGDLN VGAVLILPDG FEIAPPDRIP
     EEMKAKVGKL YFQPYSAEKK TIFVVGPVPG KKYSEMVFPI LSPDPAKTKS ISYLKYPIYV
     GGNRGRGQVY PDGSKSNNTI FTASAAGKIT AIEPAGKKGG YTLTIETANG ESISEKLPPG
     PELVVNIGDI VGVDQALTTN PNVGGFGQGE TEVVLQNPLR IQGLLVFFLF VLLAQVFLVL
     KKKQFEKVQL AEMNF