PSBA2_SYNY3
ID PSBA2_SYNY3 Reviewed; 360 AA.
AC P16033;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Photosystem II protein D1 2 {ECO:0000255|HAMAP-Rule:MF_01379};
DE Short=PSII D1 protein 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01379};
DE Flags: Precursor;
GN Name=psbA2 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}; Synonyms=psbA-2;
GN OrderedLocusNames=slr1311;
GN and
GN Name=psbA3 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}; Synonyms=psbA-3;
GN OrderedLocusNames=sll1867;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2499875; DOI=10.1093/nar/17.10.3991;
RA Ravnikar P.D., Debus R., Sevrinck J., Saetaert P., McIntosh L.;
RT "Nucleotide sequence of a second psbA gene from the unicellular
RT cyanobacterium Synechocystis 6803.";
RL Nucleic Acids Res. 17:3991-3991(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2123543; DOI=10.1093/nar/18.22.6715;
RA Metz J., Nixon P., Diner B.;
RT "Nucleotide sequence of the psbA3 gene from the cyanobacterium
RT Synechocystis PCC 6803.";
RL Nucleic Acids Res. 18:6715-6715(1990).
RN [3]
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 [4]
RP MUTAGENESIS OF PHE-255; SER-264 AND LEU-271.
RX PubMed=1498597; DOI=10.2307/3869539;
RA Ohad N., Hirschberg J.;
RT "Mutations in the D1 subunit of photosystem II distinguish between quinone
RT and herbicide binding sites.";
RL Plant Cell 4:273-282(1992).
RN [5]
RP MUTAGENESIS OF 221-SER-SER-222; 227-THR-THR-228; TYR-237; LYS-238 AND
RP ARG-257.
RX PubMed=8068689; DOI=10.1021/bi00200a035;
RA Kless H., Oren-Shamir M., Malkin S., McIntosh L., Edelman M.;
RT "The D-E region of the D1 protein is involved in multiple quinone and
RT herbicide interactions in photosystem II.";
RL Biochemistry 33:10501-10507(1994).
RN [6]
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).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
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. {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: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01379,
CC ECO:0000269|PubMed:12069591}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01379, ECO:0000269|PubMed:12069591,
CC 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 -!- 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; X56000; CAA39472.1; -; Genomic_DNA.
DR EMBL; X13547; CAA31899.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18230.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA16586.1; -; Genomic_DNA.
DR PIR; S13112; F2YB16.
DR PDB; 6WJ6; EM; 2.58 A; A=1-360.
DR PDB; 7N8O; EM; 1.93 A; A/a=1-360.
DR PDB; 7RCV; EM; 2.01 A; A/a=1-360.
DR PDBsum; 6WJ6; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; P16033; -.
DR SMR; P16033; -.
DR IntAct; P16033; 5.
DR STRING; 1148.1651658; -.
DR TCDB; 3.E.2.2.2; the photosynthetic reaction center (prc) family.
DR PaxDb; P16033; -.
DR EnsemblBacteria; BAA16586; BAA16586; BAA16586.
DR EnsemblBacteria; BAA18230; BAA18230; BAA18230.
DR KEGG; syn:sll1867; -.
DR KEGG; syn:slr1311; -.
DR eggNOG; ENOG502Z87P; Bacteria.
DR InParanoid; P16033; -.
DR OMA; CQWVTDT; -.
DR PhylomeDB; P16033; -.
DR BRENDA; 1.10.3.9; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
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; -; 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 PANTHER; PTHR33149; PTHR33149; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01151; psbA; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379"
FT /id="PRO_0000090493"
FT PROPEP 345..360
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379,
FT ECO:0000305|PubMed:8034700"
FT /id="PRO_0000316429"
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 MUTAGEN 221..222
FT /note="SS->LA: Strong herbicide resistance."
FT /evidence="ECO:0000269|PubMed:8068689"
FT MUTAGEN 227..228
FT /note="TT->AA: Herbicide resistance."
FT /evidence="ECO:0000269|PubMed:8068689"
FT MUTAGEN 237
FT /note="Y->F: Weak herbicide resistance."
FT /evidence="ECO:0000269|PubMed:8068689"
FT MUTAGEN 238
FT /note="K->V: Weak herbicide resistance."
FT /evidence="ECO:0000269|PubMed:8068689"
FT MUTAGEN 255
FT /note="F->W: Herbicide resistance."
FT /evidence="ECO:0000269|PubMed:1498597"
FT MUTAGEN 257
FT /note="R->V: Herbicide resistance."
FT /evidence="ECO:0000269|PubMed:8068689"
FT MUTAGEN 264
FT /note="S->A: Strong herbicide resistance."
FT /evidence="ECO:0000269|PubMed:1498597"
FT MUTAGEN 271
FT /note="L->V,M,A,S: Herbicide resistance."
FT /evidence="ECO:0000269|PubMed:1498597"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 110..136
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 196..221
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 268..293
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 360 AA; 39721 MW; 2FE4088498A416C2 CRC64;
MTTTLQQRES ASLWEQFCQW VTSTNNRIYV GWFGTLMIPT LLTATTCFII AFIAAPPVDI
DGIREPVAGS LLYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVVFHFL
IGIFCYMGRQ WELSYRLGMR PWICVAYSAP VSAATAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTEV ESQNYGYKFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGAWPV IGIWFTAMGV STMAFNLNGF
NFNQSILDSQ GRVIGTWADV LNRANIGFEV MHERNAHNFP LDLASGEQAP VALTAPAVNG
