CYF_PROMM
ID CYF_PROMM Reviewed; 310 AA.
AC Q7V653;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytochrome f {ECO:0000255|HAMAP-Rule:MF_00610};
DE Flags: Precursor;
GN Name=petA {ECO:0000255|HAMAP-Rule:MF_00610}; OrderedLocusNames=PMT_1323;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX548175; CAE21498.1; -; Genomic_DNA.
DR RefSeq; WP_011130691.1; NC_005071.1.
DR AlphaFoldDB; Q7V653; -.
DR SMR; Q7V653; -.
DR STRING; 74547.PMT_1323; -.
DR EnsemblBacteria; CAE21498; CAE21498; PMT_1323.
DR KEGG; pmt:PMT_1323; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_033498_0_0_3; -.
DR OMA; FWAQQNY; -.
DR OrthoDB; 744890at2; -.
DR Proteomes; UP000001423; 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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00610"
FT CHAIN 24..310
FT /note="Cytochrome f"
FT /id="PRO_0000342033"
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 310 AA; 33330 MW; 4310654D54013E3B CRC64;
MRRLIPILLG SLVLSLSILV APAASWAYPF WAQQNYDNPR EATGKIVCAN CHLAQKTTQA
EVPQSVLPDS VFKAVVKIPY KKDTTEISSD GSDVPLQVGA VVMLPDGFRL APQDRWSEEI
KEETKGVFFT QYSEEKENIL LVGPLPGDNN KEIVFPILSP DPATDSSIQF GKYSIHVGGN
RGRGQILPTG EKTNNNAFTA TEAGTITSIK SGKNGESDIK LKTDSGKVIS ETIPAGPSLL
VKVDDKVEAG APLTSDPNSG GFGQLDTEVV LQNPVRIYGL LAFFVAVSLA QILLVLKKKQ
VEKVQAAEGI