UniProt functional annotation for P0A431



	UniProt functional annotation for P0A431

UniProt code: P0A431.

Organism: Thermosynechococcus elongatus (strain BP-1).

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

Function: Part of the oxygen-evolving complex associated with photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. {ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:25006873}.

Cofactor: Note=PSII binds multiple chlorophylls, carotenoids and specific lipids. {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};

Subunit: The cyanobacterial oxygen-evolving complex is composed of PsbO, PsbP, PsbQ, PsbV and PsbU. PsbP and PsbQ are not seen in the crystal structures; however there is biochemical evidence that they are part of the OEC (By similarity). 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, 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. {ECO:0000250, 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}.

Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP- Rule:MF_01378, 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}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01378, 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}; Lumenal side {ECO:0000255|HAMAP- Rule:MF_01378, 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}. Note=Associated with PSII on the lumenal side of the thylakoid membrane.

Mass spectrometry: Mass=26830; Mass_error=30; Method=MALDI; Evidence={ECO:0000269|PubMed:19219048};

Mass spectrometry: Mass=26820; Method=MALDI; Evidence={ECO:0000269|PubMed:20558739};

Similarity: Belongs to the PsbO family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


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



Function:		Part of the oxygen-evolving complex associated with photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. {ECO:0000269\|PubMed:20558739, ECO:0000269\|PubMed:21367867, ECO:0000269\|PubMed:25006873}.


Cofactor:		Note=PSII binds multiple chlorophylls, carotenoids and specific lipids. {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};
Subunit:		The cyanobacterial oxygen-evolving complex is composed of PsbO, PsbP, PsbQ, PsbV and PsbU. PsbP and PsbQ are not seen in the crystal structures; however there is biochemical evidence that they are part of the OEC (By similarity). 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, 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes. {ECO:0000250, 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}.
Subcellular location:		Cellular thylakoid membrane {ECO:0000255\|HAMAP- Rule:MF_01378, 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}; Peripheral membrane protein {ECO:0000255\|HAMAP-Rule:MF_01378, 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}; Lumenal side {ECO:0000255\|HAMAP- Rule:MF_01378, 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}. Note=Associated with PSII on the lumenal side of the thylakoid membrane.
Mass spectrometry:		Mass=26830; Mass_error=30; Method=MALDI; Evidence={ECO:0000269\|PubMed:19219048};
Mass spectrometry:		Mass=26820; Method=MALDI; Evidence={ECO:0000269\|PubMed:20558739};
Similarity:		Belongs to the PsbO family. {ECO:0000305}.