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 02-DEC-2020, entry version 165. 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; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDBsum; 6WJ6; -. DR SMR; P16033; -. DR IntAct; P16033; 5. DR STRING; 1148.1653315; -. 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; FLIGCAC; -. DR PhylomeDB; P16033; -. 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:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB. DR GO; GO:0042651; C: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:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro. DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW. DR CDD; cd09289; Photosystem-II_D1; 1. DR Gene3D; 1.20.85.10; -; 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 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 REGION 264..265 FT /note="Quinone (B)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 118 FT /note="Magnesium (chlorophyll-a ChlzD1 axial ligand); via FT tele nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 170 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 170 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 189 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 198 FT /note="Magnesium (chlorophyll-a PD1 axial ligand); via tele FT nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 215 FT /note="Iron; shared with heterodimeric partner; via tele FT nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 272 FT /note="Iron; shared with heterodimeric partner; via tele FT nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 332 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; FT via tele nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 333 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 333 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 342 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 342 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 344 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via FT carboxylate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT METAL 344 FT /note="Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; FT via carboxylate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 126 FT /note="Pheophytin D1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01379" FT BINDING 215 FT /note="Quinone (B)" 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" 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 //