ID K9XVZ1_STAC7 Unreviewed; 222 AA.
AC K9XVZ1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Cytochrome b6 {ECO:0000256|ARBA:ARBA00035697, ECO:0000256|HAMAP-Rule:MF_00633};
GN Name=petB {ECO:0000256|HAMAP-Rule:MF_00633};
GN OrderedLocusNames=Sta7437_2708 {ECO:0000313|EMBL:AFZ36234.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ36234.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:0000256|ARBA:ARBA00003068, ECO:0000256|HAMAP-Rule:MF_00633}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00633};
CC Note=Binds 2 heme b groups non-covalently with two histidine residues
CC as axial ligands. {ECO:0000256|HAMAP-Rule:MF_00633};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00633};
CC Note=Binds one heme group covalently by a single cysteine link with no
CC axial amino acid ligand. This heme was named heme ci.
CC {ECO:0000256|HAMAP-Rule:MF_00633};
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:0000256|ARBA:ARBA00025834,
CC ECO:0000256|HAMAP-Rule:MF_00633}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_00633}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00633}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- MISCELLANEOUS: Heme 1 (or BH or b566) is high-potential and absorbs at
CC about 566 nm, and heme 2 (or BL or b562) is low-potential and absorbs
CC at about 562 nm. {ECO:0000256|HAMAP-Rule:MF_00633}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. PetB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00633}.
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DR EMBL; CP003653; AFZ36234.1; -; Genomic_DNA.
DR RefSeq; WP_015193902.1; NC_019748.1.
DR AlphaFoldDB; K9XVZ1; -.
DR STRING; 111780.Sta7437_2708; -.
DR KEGG; scs:Sta7437_2708; -.
DR PATRIC; fig|111780.3.peg.2817; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_0_2_3; -.
DR OrthoDB; 9804503at2; -.
DR Proteomes; UP000010473; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR HAMAP; MF_00633; Cytb6_f_cytb6; 1.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR023530; Cyt_B6_PetB.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR048259; Cytochrome_b_N_euk/bac.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR PANTHER; PTHR19271; CYTOCHROME B; 1.
DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF000032; Cytochrome_b6; 1.
DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00633};
KW Heme {ECO:0000256|HAMAP-Rule:MF_00633};
KW Iron {ECO:0000256|HAMAP-Rule:MF_00633};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00633};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_00633}; Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00633};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00633, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00633,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|HAMAP-Rule:MF_00633}.
FT TRANSMEM 39..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..222
FT /note="Cytochrome b/b6 N-terminal region profile"
FT /evidence="ECO:0000259|PROSITE:PS51002"
FT BINDING 42
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633"
FT BINDING 93
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633"
FT BINDING 107
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633"
FT BINDING 194
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633"
FT BINDING 209
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00633"
SQ SEQUENCE 222 AA; 25140 MW; 40C60C5F41425FAF CRC64;
MFSKQVTDSK VYQWFDERLE VQALSDDVTS KYVPPHVNIF YCLGGITLVC FLIQFATGFC
MTFYYKPTVT DAFASVEYIM NEVNFGWLIR SVHRWSASMM VLMMILHVFR VYLTGGFKKP
RELTWIAGVI MAVITVTFGV TGYSLPWDQV GYWAVKIVSG VPAAIPVVGD QMVELLRGGA
SVGQATLTRF YSLHTFVLPW LMAVFMLLHF LMIRKQGISG PL
//
