ID   CYF_SYNS9               Reviewed;         311 AA.
AC   Q3AWL6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE   Flags: Precursor;
GN   Name=petA {ECO:0000255|HAMAP-Rule:MF_00610};
GN   OrderedLocusNames=Syncc9902_1735;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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: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; CP000097; ABB26692.1; -; Genomic_DNA.
DR   RefSeq; WP_011360499.1; NC_007513.1.
DR   AlphaFoldDB; Q3AWL6; -.
DR   SMR; Q3AWL6; -.
DR   STRING; 316279.Syncc9902_1735; -.
DR   EnsemblBacteria; ABB26692; ABB26692; Syncc9902_1735.
DR   KEGG; sye:Syncc9902_1735; -.
DR   eggNOG; COG0739; Bacteria.
DR   HOGENOM; CLU_033498_0_0_3; -.
DR   OMA; FWAQQNY; -.
DR   OrthoDB; 744890at2; -.
DR   Proteomes; UP000002712; 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..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT   CHAIN           28..311
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000342038"
FT   TRANSMEM        277..297
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;  33041 MW;  279D76B61FE36F97 CRC64;
     MRRHLSLVLG SLVIGLALLI APGASWAYPF WAQQNYDSPR EATGKIVCAN CHIAKKLTQA
     EVPQSVLPDS VFTASVKVPY EEGIKEIGAD GSEVQLQVGA VVMLPDGFTL APQDRWTDEI
     KEETEGVYFT QYSDEQPNIL LVGPIPGDQN QEIVFPVLSP DPATDSNIHF GKYQIHVGGN
     RGRGQVYPTG EKSNNTVFTA PAEGKVASID AGDNGASVVT IQAADGTSTS ETIPVGPQLL
     VNVGDSVAAG DAITNDPNVG GFGQVDAEIV LQNPVRIYGL LAFFAAVAIA QIMLVLKKRQ
     IEKVQAAEGN F