ID   PSBA1_SYNY3             Reviewed;         360 AA.
AC   P07826; P74710;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Photosystem II protein D1 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            Short=PSII D1 protein 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE            EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   AltName: Full=Photosystem II Q(B) protein 1 {ECO:0000255|HAMAP-Rule:MF_01379};
DE   Flags: Precursor;
GN   Name=psbA1 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
GN   Synonyms=psbA-1; OrderedLocusNames=slr1181;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3122184; DOI=10.1093/nar/15.24.10585;
RA   Osiewacz H.D., McIntosh L.;
RT   "Nucleotide sequence of a member of the psbA multigene family from the
RT   unicellular cyanobacterium Synechocystis 6803.";
RL   Nucleic Acids Res. 15:10585-10585(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   SUBCELLULAR LOCATION, AND LACK OF PHOSPHORYLATION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=9512353; DOI=10.1016/s0014-5793(98)00088-x;
RA   Pursiheimo S., Rintamaeki E., Baena-Gonzalez E., Aro E.-M.;
RT   "Thylakoid protein phosphorylation in evolutionally divergent species with
RT   oxygenic photosynthesis.";
RL   FEBS Lett. 423:178-182(1998).
RN   [4]
RP   PROBABLE CLEAVAGE.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8034700; DOI=10.1016/s0021-9258(17)32175-0;
RA   Shestakov S.V., Anbudurai P.R., Stanbekova G.E., Gadzhiev A., Lind L.K.,
RA   Pakrasi H.B.;
RT   "Molecular cloning and characterization of the ctpA gene encoding a
RT   carboxyl-terminal processing protease. Analysis of a spontaneous
RT   photosystem II-deficient mutant strain of the cyanobacterium Synechocystis
RT   sp. PCC 6803.";
RL   J. Biol. Chem. 269:19354-19359(1994).
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:0000255|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:0000255|HAMAP-Rule:MF_01379};
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. D1 provides most of
CC       the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex
CC       (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is
CC       required for oxygen evolution. The PSII complex binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC       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, PsbZ, Psb30/Ycf12, peripheral proteins PsbO, CyanoQ (PsbQ),
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01379, ECO:0000305|PubMed:9512353}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305|PubMed:9512353}.
CC   -!- PTM: C-terminally processed by CtpA; processing is essential to allow
CC       assembly of the oxygen-evolving complex and photosynthetic growth.
CC       {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305|PubMed:8034700}.
CC   -!- PTM: Tyr-161 forms a radical intermediate that is referred to as redox-
CC       active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.
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:0000255|HAMAP-Rule:MF_01379}.
CC   -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of the
CC       psbA gene. {ECO:0000255|HAMAP-Rule:MF_01379,
CC       ECO:0000269|PubMed:8905231}.
CC   -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and ChlD2)
CC       are entirely coordinated by water. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01379}.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000255|HAMAP-Rule:MF_01379}.
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DR   EMBL; Y00885; CAA68778.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18829.1; -; Genomic_DNA.
DR   PIR; S76917; F2YB13.
DR   AlphaFoldDB; P07826; -.
DR   SMR; P07826; -.
DR   IntAct; P07826; 2.
DR   STRING; 1148.gene:10500601; -.
DR   PaxDb; 1148-1653919; -.
DR   EnsemblBacteria; BAA18829; BAA18829; BAA18829.
DR   KEGG; syn:slr1181; -.
DR   eggNOG; ENOG502Z87P; Bacteria.
DR   InParanoid; P07826; -.
DR   PhylomeDB; P07826; -.
DR   BioCyc; MetaCyc:PSBA1-MONOMER; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0009523; C:photosystem II; IBA:GO_Central.
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   Gene3D; 1.20.85.10; Photosystem II protein D1-like; 2.
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   1: Evidence at protein level;
KW   Calcium; Chlorophyll; Chromophore; Electron transport;
KW   Herbicide resistance; Iron; Magnesium; Manganese; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem II; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..344
FT                   /note="Photosystem II protein D1 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT                   /id="PRO_0000090492"
FT   PROPEP          345..360
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000305|PubMed:8034700"
FT                   /id="PRO_0000316428"
FT   TRANSMEM        29..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        118..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        142..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        197..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   TRANSMEM        274..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         118
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:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         126
FT                   /ligand="pheophytin a"
FT                   /ligand_id="ChEBI:CHEBI:136840"
FT                   /ligand_label="D1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         170
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         189
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         198
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:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         215
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         264..265
FT                   /ligand="a quinone"
FT                   /ligand_id="ChEBI:CHEBI:132124"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         272
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         332
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         333
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         342
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   BINDING         344
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            161
FT                   /note="Tyrosine radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            190
FT                   /note="Stabilizes free radical intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT   SITE            344..345
FT                   /note="Cleavage; by CtpA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT                   ECO:0000305|PubMed:8034700"
FT   CONFLICT        90
FT                   /note="G -> A (in Ref. 1; CAA68778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="I -> N (in Ref. 1; CAA68778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="F -> S (in Ref. 1; CAA68778)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  39651 MW;  41A74A7819FE90D2 CRC64;
     MTTTQLGLQE QSLWSRFCCW ITSTSNRLYI GWFGVLMIPT LLTATTCFII AFIAAPPVDI
     DGIREPIAGS LLYGNNIITA AVVPSSNAIG LHFYPIWEAH SLDEWLYNGG PYQLIVFHFL
     IGIFCYLGRQ WELSYRLGMR PWICVAYSAP VAAATATLLI YSIGQGSFSD GLPLGISGTF
     NFMLVLQAEH NVLMHPFHML GVAGVFGGAL FAAMHGSLVT SSLIRETTEV ESQNQGYKFG
     QEEETYNIVA AHGYFGRLIF QYASFNNSRA LHFFLGAWPV VGIWFAALAV CCFAFNLNGF
     NFNQSILDAQ GRPVSTWADV INRANIGFEV MHERNVHNFP LDLASGDAQM VALNAPAIEG
//