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-JUL-2019, entry version 157. 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}; GN Synonyms=psbA-2; OrderedLocusNames=slr1311; GN and GN Name=psbA3 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305}; GN Synonyms=psbA-3; OrderedLocusNames=sll1867; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; OC 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., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire 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=10.1105/tpc.4.3.273; RA Ohad N., Hirschberg J.; RT "Mutations in the D1 subunit of photosystem II distinguish between RT quinone 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., RA Lind L.K., 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 RT Synechocystis 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 RT with oxygenic photosynthesis."; RL FEBS Lett. 423:178-182(1998). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR RP 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., RA Satoh K., Pakrasi H.B.; RT "Proteomic analysis of a highly active photosystem II preparation from RT the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of RT novel polypeptides."; RL Biochemistry 41:8004-8012(2002). CC -!- FUNCTION: Photosystem II (PSII) is a light-driven CC water:plastoquinone oxidoreductase that uses light energy to CC abstract electrons from H(2)O, generating O(2) and a proton CC gradient subsequently used for ATP formation. It consists of a CC core antenna complex that captures photons, and an electron CC transfer chain that converts photonic excitation into a charge CC 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 + CC O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA- CC COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; CC EC=1.10.3.9; 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. CC It shares a non-heme iron and each subunit binds pheophytin, CC quinone, additional chlorophylls, carotenoids and lipids. D1 CC provides most of the ligands for the Mn4-Ca-O5 cluster of the CC oxygen-evolving complex (OEC). There is also a Cl(-1) ion CC associated with D1 and D2, which is required for oxygen evolution. CC The PSII complex binds additional chlorophylls, carotenoids and CC specific lipids. {ECO:0000255|HAMAP-Rule:MF_01379}; CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of CC membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, CC PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 CC peripheral proteins PsbO, PsbU, PsbV and a large number of CC cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP- CC Rule:MF_01379, ECO:0000269|PubMed:12069591}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000255|HAMAP-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 CC allow assembly of the oxygen-evolving complex and photosynthetic CC growth. {ECO:0000255|HAMAP-Rule:MF_01379, CC ECO:0000305|PubMed:8034700}. CC -!- PTM: Tyr-161 forms a radical intermediate that is referred to as CC redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}. CC -!- PTM: C-terminally processed by CtpA; processing is essential to CC allow assembly of the oxygen-evolving complex and thus CC photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of CC the psbA gene. {ECO:0000255|HAMAP-Rule:MF_01379}. CC -!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and CC ChlD2) are entirely coordinated by water. {ECO:0000255|HAMAP- CC Rule:MF_01379}. CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind in the Q(B) binding site and block subsequent electron CC transfer. {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 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 PRIDE; P16033; -. DR EnsemblBacteria; BAA16586; BAA16586; BAA16586. DR EnsemblBacteria; BAA18230; BAA18230; BAA18230. DR KEGG; syn:sll1867; -. DR KEGG; syn:slr1311; -. DR HOGENOM; HOG000246913; -. DR InParanoid; P16033; -. DR KO; K02703; -. DR OMA; GIWFTSM; -. DR PhylomeDB; P16033; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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: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 Calcium; Chlorophyll; Chromophore; Complete proteome; KW Electron transport; Herbicide resistance; Iron; Magnesium; Manganese; KW Membrane; Metal-binding; Oxidoreductase; Photosynthesis; KW Photosystem II; Reference proteome; Thylakoid; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 344 Photosystem II protein D1 2. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT /FTId=PRO_0000090493. FT PROPEP 345 360 {ECO:0000255|HAMAP-Rule:MF_01379, FT ECO:0000305|PubMed:8034700}. FT /FTId=PRO_0000316429. FT TRANSMEM 29 46 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 118 133 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 142 156 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 197 218 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT TRANSMEM 274 288 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT REGION 264 265 Quinone (B). {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 118 118 Magnesium (chlorophyll-a ChlzD1 axial FT ligand); via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 189 189 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 198 198 Magnesium (chlorophyll-a PD1 axial FT ligand); via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 215 215 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 272 272 Iron; shared with heterodimeric partner; FT via tele nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 332 332 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 3. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 4. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O]; FT calcium; via carboxylate. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O]; FT manganese 2; via carboxylate. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT BINDING 126 126 Pheophytin D1. {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT BINDING 215 215 Quinone (B). {ECO:0000255|HAMAP- FT Rule:MF_01379}. FT SITE 161 161 Tyrosine radical intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT SITE 190 190 Stabilizes free radical intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01379}. FT SITE 344 345 Cleavage; by CtpA. {ECO:0000255|HAMAP- FT Rule:MF_01379, FT ECO:0000305|PubMed:8034700}. FT MUTAGEN 221 222 SS->LA: Strong herbicide resistance. FT {ECO:0000269|PubMed:8068689}. FT MUTAGEN 227 228 TT->AA: Herbicide resistance. FT {ECO:0000269|PubMed:8068689}. FT MUTAGEN 237 237 Y->F: Weak herbicide resistance. FT {ECO:0000269|PubMed:8068689}. FT MUTAGEN 238 238 K->V: Weak herbicide resistance. FT {ECO:0000269|PubMed:8068689}. FT MUTAGEN 255 255 F->W: Herbicide resistance. FT {ECO:0000269|PubMed:1498597}. FT MUTAGEN 257 257 R->V: Herbicide resistance. FT {ECO:0000269|PubMed:8068689}. FT MUTAGEN 264 264 S->A: Strong herbicide resistance. FT {ECO:0000269|PubMed:1498597}. FT MUTAGEN 271 271 L->V,M,A,S: Herbicide resistance. FT {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 //