UniProt functional annotation for P0A444



	UniProt functional annotation for P0A444

UniProt code: P0A444.

Organism: Thermosynechococcus elongatus (strain BP-1).

Taxonomy: Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Thermosynechococcus.

Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:25006873}.

Catalytic activity: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873};

Cofactor: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3};

Subunit: Cyanobacterial PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3}.

Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP- Rule:MF_01379, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3}; Multi-pass membrane protein {ECO:0000255|HAMAP- Rule:MF_01379, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref.3}.

Ptm: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.

Ptm: Tyr-161 forms a radical intermediate that is referred to as redox- active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000303|PubMed:11217865, ECO:0000303|PubMed:14764885, ECO:0000303|PubMed:19219048, ECO:0000303|PubMed:21367867, ECO:0000303|Ref.3}.

Mass spectrometry: Mass=38144; Mass_error=224; Method=MALDI; Note=Mass for C-terminally truncated D1. The measured protein is probably a mixture of the products of the 3 psbA genes.; Evidence={ECO:0000269|PubMed:19219048};

Miscellaneous: 2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048}.

Miscellaneous: Herbicides such as terbutryn, atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:21367867}.

Miscellaneous: Cyanobacteria usually contain more than 2 copies of the psbA gene; this strain encodes 3. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:12240834}.

Similarity: Belongs to the reaction center PufL/M/PsbA/D family. {ECO:0000255|HAMAP-Rule:MF_01379}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermosynechococcus elongatus (strain BP-1).
Taxonomy:		Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Thermosynechococcus.



Function:		Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:21367867, ECO:0000269\|PubMed:25006873}.


Catalytic activity:		Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:25006873};
Cofactor:		Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:14764885, ECO:0000269\|PubMed:16355230, ECO:0000269\|PubMed:19219048, ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:21367867, ECO:0000269\|PubMed:22665786, ECO:0000269\|PubMed:23413188, ECO:0000269\|PubMed:25006873, ECO:0000269\|PubMed:25043005, ECO:0000269\|Ref.3};
Subunit:		Cyanobacterial PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:14764885, ECO:0000269\|PubMed:16355230, ECO:0000269\|PubMed:19219048, ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:21367867, ECO:0000269\|PubMed:22665786, ECO:0000269\|PubMed:23413188, ECO:0000269\|PubMed:25006873, ECO:0000269\|PubMed:25043005, ECO:0000269\|Ref.3}.
Subcellular location:		Cellular thylakoid membrane {ECO:0000255\|HAMAP- Rule:MF_01379, ECO:0000269\|PubMed:14764885, ECO:0000269\|PubMed:16355230, ECO:0000269\|PubMed:19219048, ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:21367867, ECO:0000269\|PubMed:22665786, ECO:0000269\|PubMed:23413188, ECO:0000269\|PubMed:25006873, ECO:0000269\|PubMed:25043005, ECO:0000269\|Ref.3}; Multi-pass membrane protein {ECO:0000255\|HAMAP- Rule:MF_01379, ECO:0000269\|PubMed:14764885, ECO:0000269\|PubMed:16355230, ECO:0000269\|PubMed:19219048, ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:21367867, ECO:0000269\|PubMed:22665786, ECO:0000269\|PubMed:23413188, ECO:0000269\|PubMed:25006873, ECO:0000269\|PubMed:25043005, ECO:0000269\|Ref.3}.
Ptm:		C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255\|HAMAP-Rule:MF_01379}.
Ptm:		Tyr-161 forms a radical intermediate that is referred to as redox- active TyrZ, YZ or Y-Z. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000303\|PubMed:11217865, ECO:0000303\|PubMed:14764885, ECO:0000303\|PubMed:19219048, ECO:0000303\|PubMed:21367867, ECO:0000303\|Ref.3}.
Mass spectrometry:		Mass=38144; Mass_error=224; Method=MALDI; Note=Mass for C-terminally truncated D1. The measured protein is probably a mixture of the products of the 3 psbA genes.; Evidence={ECO:0000269\|PubMed:19219048};
Miscellaneous:		2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:16355230, ECO:0000269\|PubMed:19219048}.
Miscellaneous:		Herbicides such as terbutryn, atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:21367867}.
Miscellaneous:		Cyanobacteria usually contain more than 2 copies of the psbA gene; this strain encodes 3. {ECO:0000255\|HAMAP-Rule:MF_01379, ECO:0000269\|PubMed:12240834}.
Similarity:		Belongs to the reaction center PufL/M/PsbA/D family. {ECO:0000255\|HAMAP-Rule:MF_01379}.