ID K9P2G8_CYAGP Unreviewed; 358 AA.
AC K9P2G8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Photosystem II protein D1 {ECO:0000256|HAMAP-Rule:MF_01379};
DE Short=PSII D1 protein {ECO:0000256|HAMAP-Rule:MF_01379};
DE EC=1.10.3.9 {ECO:0000256|HAMAP-Rule:MF_01379};
DE AltName: Full=Photosystem II Q(B) protein {ECO:0000256|HAMAP-Rule:MF_01379};
GN Name=psbA {ECO:0000256|HAMAP-Rule:MF_01379};
GN OrderedLocusNames=Cyagr_0383 {ECO:0000313|EMBL:AFY27577.1};
OS Cyanobium gracile (strain ATCC 27147 / PCC 6307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Cyanobium.
OX NCBI_TaxID=292564 {ECO:0000313|EMBL:AFY27577.1, ECO:0000313|Proteomes:UP000010388};
RN [1] {ECO:0000313|Proteomes:UP000010388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27147 / PCC 6307 {ECO:0000313|Proteomes:UP000010388};
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: 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/PsbD) reaction center heterodimer
CC binds P680, the primary electron donor of PSII as well as several
CC subsequent electron acceptors. {ECO:0000256|ARBA:ARBA00037683,
CC ECO:0000256|HAMAP-Rule:MF_01379}.
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:0000256|HAMAP-Rule:MF_01379};
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, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU,
CC PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000256|ARBA:ARBA00038544}.
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, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ),
CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000256|ARBA:ARBA00004636, ECO:0000256|HAMAP-Rule:MF_01379};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004636,
CC ECO:0000256|HAMAP-Rule:MF_01379}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- PTM: C-terminally processed by CtpA; processing is essential to allow
CC assembly of the oxygen-evolving complex and thus photosynthetic growth.
CC {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- PTM: Tyr-160 forms a radical intermediate that is referred to as redox-
CC active TyrZ, YZ or Y-Z. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC are entirely coordinated by water. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- MISCELLANEOUS: Cyanobacteriota usually contain more than 2 copies of
CC the psbA gene. {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil bind
CC in the Q(B) binding site and block subsequent electron transfer.
CC {ECO:0000256|HAMAP-Rule:MF_01379}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000256|ARBA:ARBA00008204, ECO:0000256|HAMAP-Rule:MF_01379,
CC ECO:0000256|RuleBase:RU004331}.
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DR EMBL; CP003495; AFY27577.1; -; Genomic_DNA.
DR RefSeq; WP_015108033.1; NC_019675.1.
DR AlphaFoldDB; K9P2G8; -.
DR STRING; 292564.Cyagr_0383; -.
DR KEGG; cgc:Cyagr_0383; -.
DR PATRIC; fig|292564.3.peg.342; -.
DR eggNOG; ENOG502Z87P; Bacteria.
DR HOGENOM; CLU_054206_1_0_3; -.
DR OrthoDB; 505356at2; -.
DR Proteomes; UP000010388; Chromosome.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0010242; F:oxygen evolving activity; IEA:UniProtKB-EC.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR CDD; cd09289; Photosystem-II_D1; 1.
DR Gene3D; 1.20.85.10; Photosystem II protein D1-like; 1.
DR HAMAP; MF_01379; PSII_PsbA_D1; 1.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005867; PSII_D1.
DR NCBIfam; TIGR01151; psbA; 1.
DR PANTHER; PTHR33149; PHOTOSYSTEM II PROTEIN D1; 1.
DR PANTHER; PTHR33149:SF12; PHOTOSYSTEM II PROTEIN D1; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; Bacterial photosystem II reaction centre, L and M subunits; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|HAMAP-Rule:MF_01379};
KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Electron transport {ECO:0000256|HAMAP-Rule:MF_01379};
KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Iron {ECO:0000256|HAMAP-Rule:MF_01379};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01379};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01379};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01379};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01379};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Photosystem II {ECO:0000256|HAMAP-Rule:MF_01379};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01379};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01379}; Transport {ECO:0000256|HAMAP-Rule:MF_01379}.
FT CHAIN 1..343
FT /note="Photosystem II protein D1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT /id="PRO_5023480294"
FT PROPEP 344..358
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT /id="PRO_5007347311"
FT TRANSMEM 28..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 117
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="ChlzD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 125
FT /ligand="pheophytin a"
FT /ligand_id="ChEBI:CHEBI:136840"
FT /ligand_label="D1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 169
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 188
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 197
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="PD1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 214
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 263..264
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /ligand_label="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 271
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 331
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 332
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 341
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT BINDING 343
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT SITE 160
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT SITE 189
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
FT SITE 343..344
FT /note="Cleavage; by CtpA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01379"
SQ SEQUENCE 358 AA; 39381 MW; 939FEC75D28678EB CRC64;
MTTAIRSGRS ESWESFCAWV TSTNNRIYVG WFGVLMIPCL LAATICYVVA FIAAPAVDID
GIREPVAGSL MYGNNIISGA VVPSSNAIGL HFYPIWEAAS LDEWLYNGGP YQLVVFHFLI
GISAYMGRQW ELSYRLGMRP WICVAYSAPL SAAFAVFLIY PLGQGSFSDG MPLGISGTFN
FMLVFQAEHN ILMHPFHMLG VAGVFGGSLF SAMHGSLVTS SLVRETTESE SQNYGYKFGQ
EEETYNIVAA HGYFGRLIFQ YASFNNSRSL HFFLAAWPVV GIWFTSLGIS TMAFNLNGFN
FNQSVLDSQG RVVNTWADVL NRANLGFEVM HERNAHNFPL DLATVQSVPV ALQAPAIG
//
