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Protein

Photosystem II 12 kDa extrinsic protein

Gene

psbU

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H2O, generating a proton gradient subsequently used for ATP formation.UniRule annotation3 Publications

Cofactori

Note: PSII binds multiple chlorophylls, carotenoids and specific lipids.UniRule annotation10 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II 12 kDa extrinsic proteinUniRule annotation
Alternative name(s):
PS II complex 12 kDa extrinsic proteinUniRule annotation
PSII-UUniRule annotation
Gene namesi
Name:psbUUniRule annotation
Ordered Locus Names:tll2409
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030UniRule annotation1 PublicationAdd
BLAST
Chaini31 – 134104Photosystem II 12 kDa extrinsic proteinPRO_0000029602Add
BLAST

Interactioni

Subunit structurei

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.By similarity9 Publications

Protein-protein interaction databases

DIPiDIP-48501N.
STRINGi197221.tll2409.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 397Combined sources
Helixi42 – 465Combined sources
Helixi50 – 523Combined sources
Beta strandi54 – 563Combined sources
Turni57 – 593Combined sources
Helixi62 – 665Combined sources
Helixi74 – 818Combined sources
Helixi88 – 936Combined sources
Helixi99 – 1079Combined sources
Helixi108 – 1114Combined sources
Helixi119 – 1224Combined sources
Helixi123 – 1253Combined sources
Turni126 – 1283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50U/u1-134[»]
2AXTX-ray3.00U/u31-134[»]
3KZIX-ray3.60U31-134[»]
4FBYX-ray6.56U/h31-134[»]
4IXQX-ray5.70U/u1-134[»]
4IXRX-ray5.90U/u1-134[»]
4PBUX-ray5.00U/u38-134[»]
4PJ0X-ray2.44U/u1-134[»]
4RVYX-ray5.50U/u38-134[»]
4TNHX-ray4.90U/u1-134[»]
4TNIX-ray4.60U/u1-134[»]
4TNJX-ray4.50U/u1-134[»]
4TNKX-ray5.20U/u1-134[»]
4V62X-ray2.90AU/BU31-134[»]
4V82X-ray3.20AU/BU31-134[»]
5E7CX-ray4.50U/u38-134[»]
ProteinModelPortaliQ9F1L5.
SMRiQ9F1L5. Positions 30-134.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9F1L5.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsbU family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41060KK. Bacteria.
ENOG41125ZV. LUCA.
HOGENOMiHOG000023243.
KOiK02719.
OMAiLLGCWGW.
OrthoDBiEOG68SW1F.

Family and domain databases

HAMAPiMF_00589. PSII_PsbU.
InterProiIPR010527. PSII_PsbU.
[Graphical view]
PfamiPF06514. PsbU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9F1L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLGRWLAL AYFVGVSLLG WINWSAPTLA ATASTEEELV NVVDEKLGTA
60 70 80 90 100
YGEKIDLNNT NIAAFIQYRG LYPTLAKLIV KNAPYESVED VLNIPGLTER
110 120 130
QKQILRENLE HFTVTEVETA LVEGGDRYNN GLYK
Length:134
Mass (Da):15,018
Last modified:March 1, 2001 - v1
Checksum:iC75346D2DA75447F
GO

Mass spectrometryi

Molecular mass is 11649±8 Da from positions 31 - 134. Determined by MALDI. 1 Publication
Molecular mass is 11641 Da from positions 31 - 134. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052848 Genomic DNA. Translation: BAB20625.1.
BA000039 Genomic DNA. Translation: BAC09961.1.
RefSeqiNP_683199.1. NC_004113.1.
WP_011058241.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09961; BAC09961; BAC09961.
GeneIDi1010437.
KEGGitel:tll2409.
PATRICi23930306. VBITheElo119873_2532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052848 Genomic DNA. Translation: BAB20625.1.
BA000039 Genomic DNA. Translation: BAC09961.1.
RefSeqiNP_683199.1. NC_004113.1.
WP_011058241.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50U/u1-134[»]
2AXTX-ray3.00U/u31-134[»]
3KZIX-ray3.60U31-134[»]
4FBYX-ray6.56U/h31-134[»]
4IXQX-ray5.70U/u1-134[»]
4IXRX-ray5.90U/u1-134[»]
4PBUX-ray5.00U/u38-134[»]
4PJ0X-ray2.44U/u1-134[»]
4RVYX-ray5.50U/u38-134[»]
4TNHX-ray4.90U/u1-134[»]
4TNIX-ray4.60U/u1-134[»]
4TNJX-ray4.50U/u1-134[»]
4TNKX-ray5.20U/u1-134[»]
4V62X-ray2.90AU/BU31-134[»]
4V82X-ray3.20AU/BU31-134[»]
5E7CX-ray4.50U/u38-134[»]
ProteinModelPortaliQ9F1L5.
SMRiQ9F1L5. Positions 30-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48501N.
STRINGi197221.tll2409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09961; BAC09961; BAC09961.
GeneIDi1010437.
KEGGitel:tll2409.
PATRICi23930306. VBITheElo119873_2532.

Phylogenomic databases

eggNOGiENOG41060KK. Bacteria.
ENOG41125ZV. LUCA.
HOGENOMiHOG000023243.
KOiK02719.
OMAiLLGCWGW.
OrthoDBiEOG68SW1F.

Miscellaneous databases

EvolutionaryTraceiQ9F1L5.

Family and domain databases

HAMAPiMF_00589. PSII_PsbU.
InterProiIPR010527. PSII_PsbU.
[Graphical view]
PfamiPF06514. PsbU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and disruption of the psbU gene from thermophilic Thermosynechococcus (formerly Synechococcus) elongatus BP-1."
    Katoh H., Ikeuchi M.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.
  3. Cited for: PROTEIN SEQUENCE OF 31-39, COFACTOR, SUBCELLULAR LOCATION.
  4. "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 (3.5 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  5. "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 (3.0 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  6. "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) OF 31-134 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Strain: BP-1.
  7. "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) OF 31-134 IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Strain: BP-1.
  8. "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) OF 31-134 IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 31-134 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  11. "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 38-134 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.

Entry informationi

Entry nameiPSBU_THEEB
AccessioniPrimary (citable) accession number: Q9F1L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.