ID   CYF_PROM5               Reviewed;         317 AA.
AC   A2BVC3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610}; OrderedLocusNames=P9515_05251;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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. {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; CP000552; ABM71734.1; -; Genomic_DNA.
DR   RefSeq; WP_011819842.1; NC_008817.1.
DR   AlphaFoldDB; A2BVC3; -.
DR   SMR; A2BVC3; -.
DR   STRING; 167542.P9515_05251; -.
DR   EnsemblBacteria; ABM71734; ABM71734; P9515_05251.
DR   KEGG; pmc:P9515_05251; -.
DR   eggNOG; COG3258; Bacteria.
DR   HOGENOM; CLU_033498_0_0_3; -.
DR   OMA; FWAQQNY; -.
DR   OrthoDB; 744890at2; -.
DR   Proteomes; UP000001589; Chromosome.
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..34
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           35..317
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000342034"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         35
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         55
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         58
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   BINDING         59
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   317 AA;  34565 MW;  C7A4731AA709C984 CRC64;
     MINFKKQIMK KTTFFLCAML LVSSILIAPR SSLAYPFWAQ QNYESPREAT GKIVCANCHL
     AQMPTIAEVP QAVGADSVFK AVVKIPYKDD IKEIGADGSE VPLQVGAVVM LPDGFKLAPQ
     ERWTDEIKEE TEGVYFTNYS EEKENIIIVG PLPGDTNKEI IFPVLSPNPA TNKEYHYGKY
     SLHIGGNRGR GQVYPTGDKS NNVIFTSSSA GTINSIETIE DGSYQINIEN ENGEITTEAV
     PVGPKLIVKE QDQITVGAPL TSDPNVGGFG QLDAEVVLQS PYRIIGLIAF FIGVGLTQIL
     LVLKKKQVEK VQAAEGI