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UniProtKB - Q8DIF8 (PSBC_THEVB)
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>sp|Q8DIF8|PSBC_THEVB Photosystem II CP43 reaction center protein OS=Thermosynechococcus vestitus (strain IAM M-273 / NIES-2133 / BP-1) OX=197221 GN=psbC PE=1 SV=2 MVTLSSNSIFATNRDQESSGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMTLFEL AHFIPEKPMYEQGLILIPHIATLGWGVGPGGEVVDTFPFFVVGVVHLISSAVLGFGGVYH AIRGPETLEEYSSFFGYDWKDKNKMTTILGFHLIVLGIGALLLVAKAMFFGGLYDTWAPG GGDVRVITNPTLDPRVIFGYLLKSPFGGEGWIVSVNNLEDVVGGHIWIGLICIAGGIWHI LTTPFGWARRAFIWSGEAYLSYSLGALSMMGFIATCFVWFNNTVYPSEFYGPTGPEASQA QAMTFLIRDQKLGANVGSAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWLEPLRGP NGLDLNKIKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINSVNFVSPRSWLATSHFV LAFFFLVGHLWHAGRARAAAAGFEKGIDRESEPVLSMPSLDCommunity curation ()Add a publicationFeedback
Protein
Photosystem II CP43 reaction center protein
Gene
psbC
Organism
Thermosynechococcus vestitus (strain IAM M-273 / NIES-2133 / BP-1)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H2O, generating O2 and a proton gradient subsequently used for ATP formation.
UniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6 A resolution."
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W., Zouni A.
J. Biol. Chem. 285:26255-26262(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.7"Structural basis of cyanobacterial photosystem II inhibition by the herbicide terbutryn."
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J., Muh F., Dau H., Saenger W., Zouni A.
J. Biol. Chem. 286:15964-15972(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.11"Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy."
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J., Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G., Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A., Gloeckner C. , Lampe A., DiFiore D., Milathianaki D., Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.
Nat. Commun. 5:4371-4371(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Note: Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.UniRule annotation
Manual assertion according to rulesi
10 PublicationsManual assertion based on experiment ini
- Ref.2"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster."
Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.
Phys. Chem. Chem. Phys. 6:4733-4736(2004)Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.3"Architecture of the photosynthetic oxygen-evolving center."
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.
Science 303:1831-1838(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II."
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.
Nature 438:1040-1044(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.5"Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride."
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.
Nat. Struct. Mol. Biol. 16:334-342(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY. - Ref.6"Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6 A resolution."
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W., Zouni A.
J. Biol. Chem. 285:26255-26262(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.7"Structural basis of cyanobacterial photosystem II inhibition by the herbicide terbutryn."
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J., Muh F., Dau H., Saenger W., Zouni A.
J. Biol. Chem. 286:15964-15972(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.8"Room temperature femtosecond X-ray diffraction of photosystem II microcrystals."
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H., Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B., Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A., DiFiore D., Fry A.R. , Messerschmidt M., Miahnahri A., Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J., Yachandra V.K.
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBCELLULAR LOCATION. - Ref.9"Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature."
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N., Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D., Fry A.R. , Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K., Bergmann U., Yano J.
Science 340:491-495(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.10"Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser."
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L. , Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C., Fromme P.
Nature 513:261-265(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 7-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.11"Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy."
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J., Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G., Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A., Gloeckner C. , Lampe A., DiFiore D., Milathianaki D., Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.
Nat. Commun. 5:4371-4371(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 355 | Mn 2 in calcium-manganese-oxide [Ca-4Mn-5O]7 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 355 | Mn 3 in calcium-manganese-oxide [Ca-4Mn-5O]7 Publications Manual assertion based on opinion ini
Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- chlorophyll binding Source: UniProtKB-UniRule
- electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Source: InterPro
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- photosynthetic electron transport in photosystem II Source: InterPro
- protein-chromophore linkage Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Biological process | Photosynthesis |
| Ligand | Chlorophyll, Chromophore, Manganese, Metal-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Photosystem II CP43 reaction center proteinUniRule annotationManual assertion according to rulesi Alternative name(s): PSII 43 kDa proteinUniRule annotation Manual assertion according to rulesi Protein CP-43UniRule annotation Manual assertion according to rulesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:psbCUniRule annotation Manual assertion according to rulesi Ordered Locus Names:tlr1631 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Thermosynechococcus vestitus (strain IAM M-273 / NIES-2133 / BP-1) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 197221 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Terrabacteria group › Cyanobacteria/Melainabacteria group › Cyanobacteria › Pseudanabaenales › Thermosynechococcaceae › Thermosynechococcus › Thermosynechococcus vestitus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Other locations
- Cellular thylakoid membrane UniRule annotation
Manual assertion according to rulesi
10 PublicationsManual assertion based on experiment ini
- Ref.2"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster."
Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.
Phys. Chem. Chem. Phys. 6:4733-4736(2004)Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.3"Architecture of the photosynthetic oxygen-evolving center."
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.
Science 303:1831-1838(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II."
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.
Nature 438:1040-1044(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.5"Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride."
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.
Nat. Struct. Mol. Biol. 16:334-342(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY. - Ref.6"Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6 A resolution."
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W., Zouni A.
J. Biol. Chem. 285:26255-26262(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.7"Structural basis of cyanobacterial photosystem II inhibition by the herbicide terbutryn."
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J., Muh F., Dau H., Saenger W., Zouni A.
J. Biol. Chem. 286:15964-15972(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.8"Room temperature femtosecond X-ray diffraction of photosystem II microcrystals."
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H., Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B., Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A., DiFiore D., Fry A.R. , Messerschmidt M., Miahnahri A., Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J., Yachandra V.K.
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBCELLULAR LOCATION. - Ref.9"Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature."
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N., Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D., Fry A.R. , Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K., Bergmann U., Yano J.
Science 340:491-495(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.10"Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser."
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L. , Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C., Fromme P.
Nature 513:261-265(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 7-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.11"Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy."
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J., Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G., Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A., Gloeckner C. , Lampe A., DiFiore D., Milathianaki D., Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.
Nat. Commun. 5:4371-4371(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
Manual assertion according to rulesi
10 PublicationsManual assertion based on experiment ini
- Ref.2"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster."
Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.
Phys. Chem. Chem. Phys. 6:4733-4736(2004)Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.3"Architecture of the photosynthetic oxygen-evolving center."
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.
Science 303:1831-1838(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II."
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.
Nature 438:1040-1044(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.5"Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride."
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.
Nat. Struct. Mol. Biol. 16:334-342(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY. - Ref.6"Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6 A resolution."
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W., Zouni A.
J. Biol. Chem. 285:26255-26262(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.7"Structural basis of cyanobacterial photosystem II inhibition by the herbicide terbutryn."
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J., Muh F., Dau H., Saenger W., Zouni A.
J. Biol. Chem. 286:15964-15972(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.8"Room temperature femtosecond X-ray diffraction of photosystem II microcrystals."
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H., Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B., Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A., DiFiore D., Fry A.R. , Messerschmidt M., Miahnahri A., Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J., Yachandra V.K.
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBCELLULAR LOCATION. - Ref.9"Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature."
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N., Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D., Fry A.R. , Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K., Bergmann U., Yano J.
Science 340:491-495(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.10"Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser."
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L. , Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C., Fromme P.
Nature 513:261-265(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 7-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.11"Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy."
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J., Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G., Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A., Gloeckner C. , Lampe A., DiFiore D., Milathianaki D., Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.
Nat. Commun. 5:4371-4371(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
- Cellular thylakoid membrane UniRule annotation
Plasma Membrane
- plasma membrane-derived thylakoid membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
- photosystem II Source: UniProtKB-KW
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 38 | Cytoplasmic1 Publication Manual assertion based on experiment ini
| 38 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 39 – 53 | Helical1 Publication Manual assertion based on experiment ini
| 15 | |
| Topological domaini | 54 – 104 | Lumenal1 Publication Manual assertion based on experiment ini
| 51 | |
| Transmembranei | 105 – 118 | Helical1 Publication Manual assertion based on experiment ini
| 14 | |
| Topological domaini | 119 – 147 | Cytoplasmic1 Publication Manual assertion based on experiment ini
| 29 | |
| Transmembranei | 148 – 161 | Helical1 Publication Manual assertion based on experiment ini
| 14 | |
| Topological domaini | 162 – 226 | Lumenal1 Publication Manual assertion based on experiment ini
| 65 | |
| Transmembranei | 227 – 240 | Helical1 Publication Manual assertion based on experiment ini
| 14 | |
| Topological domaini | 241 – 259 | Cytoplasmic1 Publication Manual assertion based on experiment ini
| 19 | |
| Transmembranei | 260 – 273 | Helical1 Publication Manual assertion based on experiment ini
| 14 | |
| Topological domaini | 274 – 417 | Lumenal1 Publication Manual assertion based on experiment ini
| 144 | |
| Transmembranei | 418 – 432 | Helical1 Publication Manual assertion based on experiment ini
| 15 | |
| Topological domaini | 433 – 461 | Cytoplasmic1 Publication Manual assertion based on experiment ini
| 29 |
Keywords - Cellular componenti
Membrane, Photosystem II, Thylakoid<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000430807 | 1 – 461 | Photosystem II CP43 reaction center proteinAdd BLAST | 461 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
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.
UniRule annotationManual assertion according to rulesi
10 PublicationsManual assertion based on experiment ini
- Ref.2"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster."
Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.
Phys. Chem. Chem. Phys. 6:4733-4736(2004)Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.3"Architecture of the photosynthetic oxygen-evolving center."
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.
Science 303:1831-1838(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.4"Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II."
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.
Nature 438:1040-1044(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.5"Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride."
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.
Nat. Struct. Mol. Biol. 16:334-342(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY. - Ref.6"Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6 A resolution."
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W., Zouni A.
J. Biol. Chem. 285:26255-26262(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.7"Structural basis of cyanobacterial photosystem II inhibition by the herbicide terbutryn."
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J., Muh F., Dau H., Saenger W., Zouni A.
J. Biol. Chem. 286:15964-15972(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.8"Room temperature femtosecond X-ray diffraction of photosystem II microcrystals."
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H., Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B., Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A., DiFiore D., Fry A.R. , Messerschmidt M., Miahnahri A., Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J., Yachandra V.K.
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBCELLULAR LOCATION. - Ref.9"Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem II at room temperature."
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N., Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D., Fry A.R. , Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K., Bergmann U., Yano J.
Science 340:491-495(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.10"Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser."
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L. , Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C., Fromme P.
Nature 513:261-265(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 7-461 IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION. - Ref.11"Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy."
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J., Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G., Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A., Gloeckner C. , Lampe A., DiFiore D., Milathianaki D., Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.
Nat. Commun. 5:4371-4371(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-48489N |
Protein interaction database and analysis system More...IntActi | Q8DIF8, 1 interactor |
STRING: functional protein association networks More...STRINGi | 197221.163937831 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 16 – 19 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 23 – 30 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 34 – 62 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 29 | |
| Helixi | 69 – 71 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 76 – 82 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 85 – 87 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 89 – 91 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 92 – 94 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 97 – 122 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 26 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 129 – 131 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 133 – 135 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 142 – 169 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 28 | |
| Beta strandi | 173 – 175 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 179 – 181 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 183 – 185 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 194 – 197 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 199 – 202 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 207 – 209 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 211 – 214 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 218 – 241 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 24 | |
| Helixi | 246 – 251 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 256 – 280 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 25 | |
| Turni | 283 – 286 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 287 – 290 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 294 – 311 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
| Turni | 316 – 318 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 324 – 331 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 337 – 339 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 341 – 346 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 352 – 354 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 355 – 357 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 360 – 363 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 365 – 370 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 374 – 384 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 395 – 398 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 399 – 401 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 410 – 441 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 32 | |
| Helixi | 449 – 451 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 453 – 456 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | Q8DIF8 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8DIF8 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q8DIF8 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the PsbB/PsbC family. PsbC subfamily.UniRule annotation
Manual assertion according to rulesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG502Z7VA, Bacteria |
Identification of Orthologs from Complete Genome Data More...OMAi | WKDKNKM |
Database of Orthologous Groups More...OrthoDBi | 166907at2 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.670, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_01496, PSII_PsbC_CP43, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000932, PS_antenna-like IPR036001, PS_II_antenna-like_sf IPR005869, PSII_PsbC IPR044900, PSII_PsbC_sf |
The PANTHER Classification System More...PANTHERi | PTHR33180, PTHR33180, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00421, PSII, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF161077, SSF161077, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01153, psbC, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q8DIF8-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MVTLSSNSIF ATNRDQESSG FAWWAGNARL INLSGKLLGA HVAHAGLIVF
60 70 80 90 100
WAGAMTLFEL AHFIPEKPMY EQGLILIPHI ATLGWGVGPG GEVVDTFPFF
110 120 130 140 150
VVGVVHLISS AVLGFGGVYH AIRGPETLEE YSSFFGYDWK DKNKMTTILG
160 170 180 190 200
FHLIVLGIGA LLLVAKAMFF GGLYDTWAPG GGDVRVITNP TLDPRVIFGY
210 220 230 240 250
LLKSPFGGEG WIVSVNNLED VVGGHIWIGL ICIAGGIWHI LTTPFGWARR
260 270 280 290 300
AFIWSGEAYL SYSLGALSMM GFIATCFVWF NNTVYPSEFY GPTGPEASQA
310 320 330 340 350
QAMTFLIRDQ KLGANVGSAQ GPTGLGKYLM RSPTGEIIFG GETMRFWDFR
360 370 380 390 400
GPWLEPLRGP NGLDLNKIKN DIQPWQERRA AEYMTHAPLG SLNSVGGVAT
410 420 430 440 450
EINSVNFVSP RSWLATSHFV LAFFFLVGHL WHAGRARAAA AGFEKGIDRE
460
SEPVLSMPSL D
Length:461
Mass (Da):50,245
Last modified:February 5, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i6A07B683DCB519B7
<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
Molecular mass is 51704±87 Da. Determined by MALDI. 1 Publication
Manual assertion based on experiment ini
- Ref.5"Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride."
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.
Nat. Struct. Mol. Biol. 16:334-342(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II WITH MANGANESE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | BA000039 Genomic DNA Translation: BAC09183.2 |
NCBI Reference Sequences More...RefSeqi | NP_682421.1, NC_004113.1 WP_024124637.1, NC_004113.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | BAC09183; BAC09183; BAC09183 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | tel:tlr1631 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|197221.4.peg.1711 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8DIF8 | Photosystem II CP43 reaction center protein | 461 | UniRef100_Q8DIF8 | |||
| Photosystem II CP43 reaction center protein | 461 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8DIF8 | Photosystem II CP43 reaction center protein (Fragment) | ) | 451 | UniRef90_Q8DIF8 | ||
| Photosystem II CP43 reaction center protein | 461 | |||||
| Photosystem II CP43 reaction center protein | 461 | |||||
| Photosystem II CP43 reaction center protein | 473 | |||||
| Photosystem II CP43 reaction center protein | 461 | |||||
| +6 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8DIF8 | Photosystem II CP43 reaction center protein (Fragment) | ) | 451 | UniRef50_Q8DIF8 | ||
| Photosystem II CP43 reaction center protein | 473 | |||||
| Photosystem II CP43 reaction center protein | 473 | |||||
| Photosystem II CP43 reaction center protein | 473 | |||||
| Photosystem II CP43 reaction center protein | 473 | |||||
| +6460 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000039 Genomic DNA Translation: BAC09183.2 |
| RefSeqi | NP_682421.1, NC_004113.1 WP_024124637.1, NC_004113.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1S5L | X-ray | 3.50 | C/c | 2-461 | [»] | |
| 1W5C | X-ray | 3.20 | C/I | 2-461 | [»] | |
| 2AXT | X-ray | 3.00 | C/c | 2-461 | [»] | |
| 3KZI | X-ray | 3.60 | C | 1-461 | [»] | |
| 4FBY | X-ray | 6.56 | C/P | 1-461 | [»] | |
| 4IXQ | X-ray | 5.70 | C/c | 1-461 | [»] | |
| 4IXR | X-ray | 5.90 | C/c | 1-461 | [»] | |
| 4PBU | X-ray | 5.00 | C/c | 7-461 | [»] | |
| 4PJ0 | X-ray | 2.44 | C/c | 1-461 | [»] | |
| 4RVY | X-ray | 5.50 | C/c | 1-461 | [»] | |
| 4TNH | X-ray | 4.90 | C/c | 1-461 | [»] | |
| 4TNI | X-ray | 4.60 | C/c | 1-461 | [»] | |
| 4TNJ | X-ray | 4.50 | C/c | 1-461 | [»] | |
| 4TNK | X-ray | 5.20 | C/c | 1-461 | [»] | |
| 4V62 | X-ray | 2.90 | AC/BC | 1-461 | [»] | |
| 4V82 | X-ray | 3.20 | AC/BC | 1-461 | [»] | |
| 5E79 | X-ray | 3.50 | C/c | 11-461 | [»] | |
| 5E7C | X-ray | 4.50 | C/c | 11-461 | [»] | |
| 5H2F | X-ray | 2.20 | C/c | 7-461 | [»] | |
| 5KAF | X-ray | 3.00 | C/c | 1-461 | [»] | |
| 5KAI | X-ray | 2.80 | C/c | 1-461 | [»] | |
| 5MX2 | X-ray | 2.20 | C/c | 1-461 | [»] | |
| 5TIS | X-ray | 2.25 | C/c | 1-461 | [»] | |
| 5ZZN | X-ray | 2.10 | C/c | 7-461 | [»] | |
| 6DHE | X-ray | 2.05 | C/c | 11-461 | [»] | |
| 6DHF | X-ray | 2.08 | C/c | 11-461 | [»] | |
| 6DHG | X-ray | 2.50 | C/c | 11-461 | [»] | |
| 6DHH | X-ray | 2.20 | C/c | 11-461 | [»] | |
| 6DHO | X-ray | 2.07 | C/c | 11-461 | [»] | |
| 6DHP | X-ray | 2.04 | C/c | 11-461 | [»] | |
| 6W1O | X-ray | 2.08 | C/c | 1-461 | [»] | |
| 6W1P | X-ray | 2.26 | C/c | 1-461 | [»] | |
| 6W1Q | X-ray | 2.27 | C/c | 1-461 | [»] | |
| 6W1R | X-ray | 2.23 | C/c | 1-461 | [»] | |
| 6W1T | X-ray | 2.01 | C/c | 1-461 | [»] | |
| 6W1U | X-ray | 2.09 | C/c | 1-461 | [»] | |
| 6W1V | X-ray | 2.09 | C/c | 1-461 | [»] | |
| 7NHO | electron microscopy | 2.66 | C | 1-461 | [»] | |
| 7NHP | electron microscopy | 2.72 | C | 1-461 | [»] | |
| 7NHQ | electron microscopy | 2.68 | C | 1-461 | [»] | |
| 7RF1 | X-ray | 1.89 | C/c | 1-461 | [»] | |
| 7RF2 | X-ray | 2.08 | C/c | 1-461 | [»] | |
| 7RF3 | X-ray | 2.26 | C/c | 1-461 | [»] | |
| 7RF4 | X-ray | 2.27 | C/c | 1-461 | [»] | |
| 7RF5 | X-ray | 2.23 | C/c | 1-461 | [»] | |
| 7RF6 | X-ray | 2.01 | C/c | 1-461 | [»] | |
| 7RF7 | X-ray | 2.09 | C/c | 1-461 | [»] | |
| 7RF8 | X-ray | 2.09 | C/c | 1-461 | [»] | |
| AlphaFoldDBi | Q8DIF8 | |||||
| SMRi | Q8DIF8 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| DIPi | DIP-48489N |
| IntActi | Q8DIF8, 1 interactor |
| STRINGi | 197221.163937831 |
Genome annotation databases
| EnsemblBacteriai | BAC09183; BAC09183; BAC09183 |
| KEGGi | tel:tlr1631 |
| PATRICi | fig|197221.4.peg.1711 |
Phylogenomic databases
| eggNOGi | ENOG502Z7VA, Bacteria |
| OMAi | WKDKNKM |
| OrthoDBi | 166907at2 |
Miscellaneous databases
| EvolutionaryTracei | Q8DIF8 |
Family and domain databases
| Gene3Di | 1.10.10.670, 1 hit |
| HAMAPi | MF_01496, PSII_PsbC_CP43, 1 hit |
| InterProi | View protein in InterPro IPR000932, PS_antenna-like IPR036001, PS_II_antenna-like_sf IPR005869, PSII_PsbC IPR044900, PSII_PsbC_sf |
| PANTHERi | PTHR33180, PTHR33180, 1 hit |
| Pfami | View protein in Pfam PF00421, PSII, 1 hit |
| SUPFAMi | SSF161077, SSF161077, 1 hit |
| TIGRFAMsi | TIGR01153, psbC, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | PSBC_THEVB | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q8DIF8Primary (citable) accession number: Q8DIF8 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 29, 2014 |
| Last sequence update: | February 5, 2008 | |
| Last modified: | May 25, 2022 | |
| This is version 122 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
