UniProt functional annotation for P0A387



	UniProt functional annotation for P0A387

UniProt code: P0A387.

Organism: Thermosynechococcus vulcanus (Synechococcus vulcanus).

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

Function: Low-potential cytochrome c that plays a role in the oxygen- evolving complex of photosystem II (PSII). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. 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:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:1314738, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8382523}.

Cofactor: Note=Binds 1 heme group covalently per subunit. PSII binds multiple chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP- Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205};

Subunit: The cyanobacterial oxygen-evolving complex is composed of PsbO, PsbP, PsbQ, PsbV and PsbU (Probable). PsbP and PsbQ are not seen in the crystal structures; however there is biochemical evidence that they are part of the OEC. 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:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12461137, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:1314738, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205}.

Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP- Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Lumenal side {ECO:0000255|HAMAP- Rule:MF_01378, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624, ECO:0000269|PubMed:8397205}. Note=Associated with photosystem II at the lumenal side of the thylakoid membrane.

Similarity: Belongs to the cytochrome c family. PsbV subfamily. {ECO:0000255|HAMAP-Rule:MF_01378}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermosynechococcus vulcanus (Synechococcus vulcanus).
Taxonomy:		Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Thermosynechococcus.



Function:		Low-potential cytochrome c that plays a role in the oxygen- evolving complex of photosystem II (PSII). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. 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:0000255\|HAMAP-Rule:MF_01378, ECO:0000269\|PubMed:1314738, ECO:0000269\|PubMed:19433803, ECO:0000269\|PubMed:23426624, ECO:0000269\|PubMed:8382523}.


Cofactor:		Note=Binds 1 heme group covalently per subunit. PSII binds multiple chlorophylls, carotenoids and specific lipids. {ECO:0000255\|HAMAP- Rule:MF_01378, ECO:0000269\|PubMed:12518057, ECO:0000269\|PubMed:19433803, ECO:0000269\|PubMed:21499260, ECO:0000269\|PubMed:23426624, ECO:0000269\|PubMed:8397205};
Subunit:		The cyanobacterial oxygen-evolving complex is composed of PsbO, PsbP, PsbQ, PsbV and PsbU (Probable). PsbP and PsbQ are not seen in the crystal structures; however there is biochemical evidence that they are part of the OEC. 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:0000255\|HAMAP-Rule:MF_01378, ECO:0000269\|PubMed:12461137, ECO:0000269\|PubMed:12518057, ECO:0000269\|PubMed:1314738, ECO:0000269\|PubMed:19433803, ECO:0000269\|PubMed:21499260, ECO:0000269\|PubMed:23426624, ECO:0000269\|PubMed:8397205}.
Subcellular location:		Cellular thylakoid membrane {ECO:0000255\|HAMAP- Rule:MF_01378, ECO:0000269\|PubMed:12518057, ECO:0000269\|PubMed:19433803, ECO:0000269\|PubMed:21499260, ECO:0000269\|PubMed:23426624}; Peripheral membrane protein {ECO:0000255\|HAMAP-Rule:MF_01378, ECO:0000269\|PubMed:12518057, ECO:0000269\|PubMed:19433803, ECO:0000269\|PubMed:21499260, ECO:0000269\|PubMed:23426624}; Lumenal side {ECO:0000255\|HAMAP- Rule:MF_01378, ECO:0000269\|PubMed:12518057, ECO:0000269\|PubMed:19433803, ECO:0000269\|PubMed:21499260, ECO:0000269\|PubMed:23426624, ECO:0000269\|PubMed:8397205}. Note=Associated with photosystem II at the lumenal side of the thylakoid membrane.
Similarity:		Belongs to the cytochrome c family. PsbV subfamily. {ECO:0000255\|HAMAP-Rule:MF_01378}.