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Protein

Photosystem II reaction center protein M

Gene

psbM

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

Functioni

One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H2O, generating O2 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. This subunit is found at the monomer-monomer interface. Probably involved in dimerization of PSII; at the monomer-monomer interface the only protein-protein contacts observed are between the 2 PsbM subunits. Lipids, chlorophylls and carotenoids contribute strongly to PSII dimerization.UniRule annotation5 Publications

Cofactori

Note: PSII binds multiple chlorophylls, carotenoids and specific lipids.10 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II reaction center protein MUniRule annotation
Short name:
PSII-MUniRule annotation
Gene namesi
Name:psbMUniRule annotation
Ordered Locus Names:tsl2052
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Lumenal1 Publication
Transmembranei9 – 2214Helical1 PublicationAdd
BLAST
Topological domaini23 – 3614Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Reaction center, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Decreased yields of PSII dimers with increased PSII monomers, slightly slower photoautotrophic growth, about 20% less oxygen evolution. Formed PSII dimers are less stable than wild-type.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3636Photosystem II reaction center protein MPRO_0000217585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-formylmethionine2 Publications

Keywords - PTMi

Formylation

Interactioni

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 annotation9 Publications

Protein-protein interaction databases

DIPiDIP-48498N.
STRINGi197221.tsl2052.

Structurei

Secondary structure

1
36
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 3024Combined sources
Helixi31 – 333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50M/m1-36[»]
2AXTX-ray3.00M/m1-36[»]
3KZIX-ray3.60M1-36[»]
4FBYX-ray6.56M/e1-36[»]
4IXQX-ray5.70M/m1-36[»]
4IXRX-ray5.90M/m1-36[»]
4PBUX-ray5.00M/m1-34[»]
4PJ0X-ray2.44M/m1-36[»]
4RVYX-ray5.50M/m1-34[»]
4TNHX-ray4.90M/m1-36[»]
4TNIX-ray4.60M/m1-36[»]
4TNJX-ray4.50M/m1-36[»]
4TNKX-ray5.20M/m1-36[»]
4V62X-ray2.90AM/BM1-36[»]
4V82X-ray3.20AM/BM1-36[»]
5E7CX-ray4.50M/m1-34[»]
ProteinModelPortaliQ8DHA7.
SMRiQ8DHA7. Positions 1-30.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DHA7.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsbM family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4106DDF. Bacteria.
ENOG410Y5C4. LUCA.
HOGENOMiHOG000054399.
KOiK02714.
OrthoDBiEOG615VRV.

Family and domain databases

HAMAPiMF_00438. PSII_PsbM.
InterProiIPR007826. PSII_PsbM.
[Graphical view]
PfamiPF05151. PsbM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03038. PS_II_psbM. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8DHA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
MEVNQLGLIA TALFVLVPSV FLIILYVQTE SQQKSS
Length:36
Mass (Da):3,981
Last modified:March 1, 2003 - v1
Checksum:iC7CE190547B00AD4
GO

Mass spectrometryi

Molecular mass is 4011±2 Da from positions 1 - 36. Determined by MALDI. 1 Publication
Molecular mass is 4009 Da from positions 1 - 36. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09604.1.
RefSeqiNP_682842.1. NC_004113.1.
WP_011057887.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09604; BAC09604; BAC09604.
GeneIDi1011591.
KEGGitel:tsl2052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09604.1.
RefSeqiNP_682842.1. NC_004113.1.
WP_011057887.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50M/m1-36[»]
2AXTX-ray3.00M/m1-36[»]
3KZIX-ray3.60M1-36[»]
4FBYX-ray6.56M/e1-36[»]
4IXQX-ray5.70M/m1-36[»]
4IXRX-ray5.90M/m1-36[»]
4PBUX-ray5.00M/m1-34[»]
4PJ0X-ray2.44M/m1-36[»]
4RVYX-ray5.50M/m1-34[»]
4TNHX-ray4.90M/m1-36[»]
4TNIX-ray4.60M/m1-36[»]
4TNJX-ray4.50M/m1-36[»]
4TNKX-ray5.20M/m1-36[»]
4V62X-ray2.90AM/BM1-36[»]
4V82X-ray3.20AM/BM1-36[»]
5E7CX-ray4.50M/m1-34[»]
ProteinModelPortaliQ8DHA7.
SMRiQ8DHA7. Positions 1-30.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48498N.
STRINGi197221.tsl2052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09604; BAC09604; BAC09604.
GeneIDi1011591.
KEGGitel:tsl2052.

Phylogenomic databases

eggNOGiENOG4106DDF. Bacteria.
ENOG410Y5C4. LUCA.
HOGENOMiHOG000054399.
KOiK02714.
OrthoDBiEOG615VRV.

Miscellaneous databases

EvolutionaryTraceiQ8DHA7.

Family and domain databases

HAMAPiMF_00438. PSII_PsbM.
InterProiIPR007826. PSII_PsbM.
[Graphical view]
PfamiPF05151. PsbM. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03038. PS_II_psbM. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.
  2. Cited for: PROTEIN SEQUENCE OF 1-15, SUBCELLULAR LOCATION.
  3. "Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with the PSII complex in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
    Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.
    Plant Cell Physiol. 48:1758-1763(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-6, COFACTOR, SUBCELLULAR LOCATION.
  4. "Roles of PsbI and PsbM in photosystem II dimer formation and stability studied by deletion mutagenesis and X-ray crystallography."
    Kawakami K., Umena Y., Iwai M., Kawabata Y., Ikeuchi M., Kamiya N., Shen J.R.
    Biochim. Biophys. Acta 1807:319-325(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "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) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  6. "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) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  7. "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, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOPOLOGY.
    Strain: BP-1.
  8. "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, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Strain: BP-1.
  9. "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, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  12. "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 1-34 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.

Entry informationi

Entry nameiPSBM_THEEB
AccessioniPrimary (citable) accession number: Q8DHA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 85 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.