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 14-MAY-2014, entry version 122. DE RecName: Full=Photosystem Q(B) protein 2; DE EC=1.10.3.9; DE AltName: Full=32 kDa thylakoid membrane protein 2; DE AltName: Full=Photosystem II protein D1 2; DE Flags: Precursor; GN Name=psbA2; Synonyms=psbA-2; OrderedLocusNames=slr1311; GN and GN Name=psbA3; Synonyms=psbA-3; OrderedLocusNames=sll1867; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; 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 FOR HERBICIDE RESISTANCE. 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 FOR HERBICIDE RESISTANCE. 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 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). CC -!- FUNCTION: This is one of the two reaction center proteins of CC photosystem II (By similarity). CC -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2 CC plastoquinol. CC -!- COFACTOR: The PsbA/B heterodimer binds P680, the primary electron CC donor of PSII. It shares a non-heme iron and each subunit binds CC additional chlorophylls and pheophytin. PsbA provides most of the CC ligands for the Mn-cluster of the oxygen-evolving complex (By CC similarity). CC -!- SUBUNIT: The PsbA/B heterodimer binds the P680 chlorophylls and CC subsequent electron acceptors. PSII consists of a core antenna CC complex that captures photons, and an electron transfer chain that CC converts photonic excitation into a charge separation. PSII forms CC dimeric complexes (By similarity). CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass CC membrane protein (Probable). CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind to Q(B) and block electron transport. CC -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of CC the psbA gene. CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family. 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 RefSeq; NP_439906.1; NC_000911.1. DR RefSeq; NP_441550.1; NC_000911.1. DR RefSeq; YP_005649961.1; NC_017277.1. DR RefSeq; YP_005651608.1; NC_017277.1. DR RefSeq; YP_007449789.1; NC_020286.1. DR RefSeq; YP_007451432.1; NC_020286.1. DR ProteinModelPortal; P16033; -. DR SMR; P16033; 10-344. DR IntAct; P16033; 5. DR STRING; 1148.slr1311; -. 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 GeneID; 12254260; -. DR GeneID; 12255303; -. DR GeneID; 14615430; -. DR GeneID; 14617092; -. DR GeneID; 951890; -. DR GeneID; 953105; -. DR KEGG; syn:sll1867; -. DR KEGG; syn:slr1311; -. DR KEGG; syy:SYNGTS_0008; -. DR KEGG; syy:SYNGTS_1655; -. DR KEGG; syz:MYO_116700; -. DR KEGG; syz:MYO_180; -. DR PATRIC; 23836870; VBISynSp132158_0010. DR eggNOG; NOG04871; -. DR HOGENOM; HOG000246913; -. DR KO; K02703; -. DR OMA; CFTIAFI; -. DR OrthoDB; EOG6Q2SGP; -. DR PhylomeDB; P16033; -. 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:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell. 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-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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; -; 1. DR HAMAP; MF_01379; PSII_PsbA_D1; 1. DR InterPro; IPR000484; Photo_RC_L/M. DR InterPro; IPR005867; PSII_D1. 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; Complete proteome; Electron transport; Herbicide resistance; KW Iron; Manganese; Membrane; Metal-binding; Oxidoreductase; KW Photosynthesis; Photosystem II; Reference proteome; Thylakoid; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 344 Photosystem Q(B) protein 2. FT /FTId=PRO_0000090493. FT PROPEP 345 360 Potential. FT /FTId=PRO_0000316429. FT TRANSMEM 36 56 Helical; (Potential). FT TRANSMEM 109 129 Helical; (Potential). FT TRANSMEM 141 164 Helical; (Potential). FT TRANSMEM 192 218 Helical; (Potential). FT TRANSMEM 269 289 Helical; (Potential). FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; calcium (By similarity). FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 1 (By similarity). FT METAL 189 189 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2 (By similarity). FT METAL 215 215 Iron; shared with heterodimeric partner FT (By similarity). FT METAL 272 272 Iron; shared with heterodimeric partner FT (By similarity). FT METAL 332 332 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2; via tele nitrogen (By FT similarity). FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 1 (By similarity). FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 3 (By similarity). FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 2 (By similarity). FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 4 (By similarity). FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; calcium; via carboxylate (By FT similarity). FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn- FT 5O]; manganese 4; via carboxylate (By FT similarity). FT SITE 344 345 Cleavage; by CtpA (By similarity). FT MUTAGEN 221 222 SS->LA: Strong herbicide resistance. FT MUTAGEN 227 228 TT->AA: Herbicide resistance. FT MUTAGEN 237 237 Y->F: Weak herbicide resistance. FT MUTAGEN 238 238 K->V: Weak herbicide resistance. FT MUTAGEN 255 255 F->W: Herbicide resistance. FT MUTAGEN 257 257 R->V: Herbicide resistance. FT MUTAGEN 264 264 S->A: Strong herbicide resistance. FT MUTAGEN 271 271 L->V,M,A,S: Herbicide resistance. 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 //