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CYB6_RIPO1
ID   CYB6_RIPO1              Reviewed;         222 AA.
AC   B7K1G1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Cytochrome b6 {ECO:0000255|HAMAP-Rule:MF_00633};
GN   Name=petB {ECO:0000255|HAMAP-Rule:MF_00633};
GN   OrderedLocusNames=PCC8801_3538;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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_00633}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00633};
CC       Note=Binds 2 heme groups. One heme group is bound covalently by a
CC       single cysteine link, the other one non-covalently. {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-
CC       Rule:MF_00633}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00633}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00633}.
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:0000255|HAMAP-Rule:MF_00633}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family. PetB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00633}.
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DR   EMBL; CP001287; ACK67503.1; -; Genomic_DNA.
DR   RefSeq; WP_012596761.1; NC_011726.1.
DR   AlphaFoldDB; B7K1G1; -.
DR   SMR; B7K1G1; -.
DR   STRING; 41431.PCC8801_3538; -.
DR   EnsemblBacteria; ACK67503; ACK67503; PCC8801_3538.
DR   KEGG; cyp:PCC8801_3538; -.
DR   eggNOG; COG1290; Bacteria.
DR   HOGENOM; CLU_031114_0_2_3; -.
DR   OMA; WATQTGM; -.
DR   OrthoDB; 1339825at2; -.
DR   Proteomes; UP000008204; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Gene3D; 1.20.810.10; -; 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; IPR016174; Di-haem_cyt_TM.
DR   PANTHER; PTHR19271:SF20; PTHR19271:SF20; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..222
FT                   /note="Cytochrome b6"
FT                   /id="PRO_1000130663"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         42
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         93
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         107
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         194
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
FT   BINDING         209
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00633"
SQ   SEQUENCE   222 AA;  25224 MW;  1CDD6A3C46DD02BE CRC64;
     MFSKQVTDSP IYKWFDNRLE IQAISDDITS KYVPPHVNIF YCLGGITLVC FIIQFATGFA
     MTFYYKPTVT DAFASVQYIM NEVNFGWLIR SIHRWSASMM VLMMILHVFR VYLTGGFKKP
     RELTWMTGVI LAVITVSFGV TGYSLPWDQV GYWAVKIVSG VPAAIPVVGD QMVELLRGGQ
     SVGQATLTRF YSLHTFVFPW LIAVFMLMHF LMIRKQGISG PL
 
 
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