ID   CYF_SYNP2               Reviewed;         325 AA.
AC   P26293; B1XQK2;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA; OrderedLocusNames=SYNPCC7002_A1910;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1421151; DOI=10.1007/bf00040607;
RA   Brand S.N., Tan X., Widger W.R.;
RT   "Cloning and sequencing of the petBD operon from the cyanobacterium
RT   Synechococcus sp. PCC 7002.";
RL   Plant Mol. Biol. 20:481-491(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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: Cellular thylakoid membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR   EMBL; M74514; AAA22070.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACA99897.1; -; Genomic_DNA.
DR   RefSeq; WP_012307520.1; NC_010475.1.
DR   AlphaFoldDB; P26293; -.
DR   SMR; P26293; -.
DR   STRING; 32049.SYNPCC7002_A1910; -.
DR   EnsemblBacteria; ACA99897; ACA99897; SYNPCC7002_A1910.
DR   KEGG; syp:SYNPCC7002_A1910; -.
DR   eggNOG; COG3258; Bacteria.
DR   HOGENOM; CLU_033498_0_0_3; -.
DR   OMA; FWAQQNY; -.
DR   Proteomes; UP000001688; 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   Reference proteome; Signal; Thylakoid; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000250"
FT   CHAIN           41..325
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000023847"
FT   TRANSMEM        290..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         41
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         62
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
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   CONFLICT        322..323
FT                   /note="QL -> NC (in Ref. 1; AAA22070)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  34875 MW;  1CF5A2C58058C8FA CRC64;
     MKTPELMAIW QRLKTACLVA IATFGLFFAS DVLFPQAAAA YPFWAQQTAP ETPREATGRI
     VCANCHLAAK EAEVEIPQSV LPDQVFEAVV KIPYDHSQQQ VLGDGSKGGL NVGAVLMLPD
     GFKIAPADRL SDELKEKTEG LYFQSYAPDQ ENVVIIGPIS GDQYEEIVFP VLSPDPKTDK
     NINYGKYAVH LGANRGRGQV YPTGELSNNN QFKASATGTI TNIAVNEAAG TDITISTEAG
     EVIDTIPAGP EVIVSEGQAI AAGEALTNNP NVGGFGQKDT EVVLQNPARI YGYMAFVAGI
     MLTQIFLVLK KKQVERVQAA GQLDF