ID   CYF_GLOVI               Reviewed;         342 AA.
AC   Q7NCE0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cytochrome f;
DE   Flags: Precursor;
GN   Name=petA; OrderedLocusNames=glr3039;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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:0000305};
CC       Note=Binds 1 heme group covalently. {ECO:0000305};
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: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Tyr/Phe in position 29 necessary for
CC       binding heme. {ECO:0000305}.
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DR   EMBL; BA000045; BAC90980.1; -; Genomic_DNA.
DR   RefSeq; NP_925985.1; NC_005125.1.
DR   RefSeq; WP_011143032.1; NC_005125.1.
DR   AlphaFoldDB; Q7NCE0; -.
DR   SMR; Q7NCE0; -.
DR   STRING; 251221.35213609; -.
DR   EnsemblBacteria; BAC90980; BAC90980; BAC90980.
DR   KEGG; gvi:glr3039; -.
DR   PATRIC; fig|251221.4.peg.3069; -.
DR   eggNOG; COG3258; Bacteria.
DR   HOGENOM; CLU_033498_0_0_3; -.
DR   InParanoid; Q7NCE0; -.
DR   OMA; FWAQQNY; -.
DR   OrthoDB; 744890at2; -.
DR   PhylomeDB; Q7NCE0; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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-KW.
DR   Gene3D; 2.60.40.830; -; 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   Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Photosynthesis; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..342
FT                   /note="Cytochrome f"
FT                   /id="PRO_0000342027"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         48
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255"
FT   BINDING         51
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   342 AA;  36650 MW;  6E4AE5B870FADFA9 CRC64;
     MKKQWIAGAF GLTAALAGLV SVPQSALAWP SFAAGYEEAR ESSGKIVCAN CHLAVKPTEI
     EVPQSVLPGK VFDLKIHVPY DTKIQQVGAD GSPAPMQIGA YIQLPEGFTV ADEKEWSAEA
     KESIEKYGGV TPLYADKPER SNILIINQID GSTVPGQEFI VPVKPPDPNA KDAKVNFGKY
     GVYVGANRGR GQVYSNGVAS NTAQYNAPVA GTISAVQTGV TFTDKLQYGL GTEATDFEYT
     NGTRVTITDE KGKASIVNIP PGPKLLDTVK QGAQIKAGQP LTNDPNVGGY GQEERDIVLQ
     DPQRVTWLVA FLAAAFICQL LLVLKKKQVE KVQEFEAQKQ GL