PSBD_BPSYP
ID PSBD_BPSYP Reviewed; 353 AA.
AC Q7Y4H2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Photosystem II D2 protein;
DE Short=PSII D2 protein;
DE EC=1.10.3.9;
DE AltName: Full=Photosystem Q(A) protein;
GN Name=psbD;
OS Synechococcus phage S-PM2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Nodensvirus; Synechococcus virus SPM2.
OX NCBI_TaxID=238854;
OH NCBI_TaxID=1129; Synechococcus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12917674; DOI=10.1038/424741a;
RA Mann N.H., Cook A., Millard A., Bailey S., Clokie M.;
RT "Marine ecosystems: bacterial photosynthesis genes in a virus.";
RL Nature 424:741-741(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15838046; DOI=10.1128/jb.187.9.3188-3200.2005;
RA Mann N.H., Clokie M.R., Millard A., Cook A., Wilson W.H., Wheatley P.J.,
RA Letarov A., Krisch H.M.;
RT "The genome of S-PM2, a 'photosynthetic' T4-type bacteriophage that infects
RT marine Synechococcus strains.";
RL J. Bacteriol. 187:3188-3200(2005).
CC -!- FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone
CC oxidoreductase that uses light energy to abstract electrons from H(2)O,
CC generating O(2) and a proton gradient subsequently used for ATP
CC formation. It consists of a core antenna complex that captures photons,
CC and an electron transfer chain that converts photonic excitation into a
CC charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer
CC binds P680, the primary electron donor of PSII as well as several
CC subsequent electron acceptors. D2 is needed for assembly of a stable
CC PSII complex. {ECO:0000250|UniProtKB:D0VWR8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2;
CC Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9;
CC Evidence={ECO:0000250|UniProtKB:D0VWR8};
CC -!- COFACTOR:
CC Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
CC primary electron donor of PSII, and subsequent electron acceptors. It
CC shares a non-heme iron and each subunit binds pheophytin, quinone,
CC additional chlorophylls, carotenoids and lipids. There is also a Cl(-1)
CC ion associated with D1 and D2, which is required for oxygen evolution.
CC The PSII complex binds additional chlorophylls, carotenoids and
CC specific lipids. {ECO:0000250|UniProtKB:D0VWR8};
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000250|UniProtKB:D0VWR8}.
CC -!- SUBCELLULAR LOCATION: Host cellular thylakoid membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000250|UniProtKB:D0VWR8}.
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DR EMBL; AY329638; AAP92670.1; -; Genomic_DNA.
DR EMBL; AJ630128; CAF34244.1; -; Genomic_DNA.
DR RefSeq; YP_195214.1; NC_006820.1.
DR SMR; Q7Y4H2; -.
DR PRIDE; Q7Y4H2; -.
DR GeneID; 10100903; -.
DR KEGG; vg:10100903; -.
DR Proteomes; UP000000994; Genome.
DR GO; GO:0044160; C:host thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR Gene3D; 1.20.85.10; -; 1.
DR HAMAP; MF_01383; PSII_PsbD_D2; 1.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005868; PSII_PsbD/D2.
DR PANTHER; PTHR33149; PTHR33149; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01152; psbD; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 3: Inferred from homology;
KW Chlorophyll; Chromophore; Electron transport; Host membrane;
KW Host thylakoid; Iron; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem II; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..353
FT /note="Photosystem II D2 protein"
FT /id="PRO_0000359710"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 125..141
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 153..166
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT TRANSMEM 279..295
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 118
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="ChlzD2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 130
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 143
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D2"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 198
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD2"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 215
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 262
FT /ligand="a plastoquinone"
FT /ligand_id="ChEBI:CHEBI:17757"
FT /ligand_label="Q(A)"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000250|UniProtKB:D0VWR8"
SQ SEQUENCE 353 AA; 39693 MW; 6A9197C13E1C557D CRC64;
MTSSTLSQPI KQRGWFDVLD DWIKRDRFVF VGWSGLLLFP TAYLALGGWL TGTTFVTSWY
THGLASSYLE GANFLTAAVS TPADAMGHSL LLLWGPESQG DIVRWFQLGG LWTFVALHGA
FSLIGFMLRQ FEISRLVGIR PYNAIAFSGP IAVFVSVFLM YPLGQSSWFF APSFGVAAIF
RFLLFLQGFH NWTLNPFHMM GVAGILGGAL LCAIHGATVE NTLYEDGEQS NTFKAFEPTQ
EEETYSMVTA NRYWSQIFGI AFSNKRWLHF FMLFVPVMGL WTSSIGIIGL ALNLRAYDFV
SQEIRAAEDP EFETFYTKNI LLNEGLRAWM APVDQPHENF VFPEEVLPRG NAL
