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Protein

Photosystem II reaction center protein Z

Gene

psbZ

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

Functioni

Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. May also aid in binding of PsbK, Ycf12 and the oxygen-evolving complex to PSII, at least in vitro. 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 annotation4 Publications

Cofactori

Note: PSII binds multiple chlorophylls, carotenoids and specific lipids.11 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II reaction center protein ZUniRule annotation
Short name:
PSII-ZUniRule annotation
Gene namesi
Name:psbZUniRule annotation
Ordered Locus Names:tsr1967
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 – 1010Lumenal
Transmembranei11 – 2414HelicalUniRule annotation1 PublicationAdd
BLAST
Topological domaini25 – 3814Cytoplasmic1 PublicationAdd
BLAST
Transmembranei39 – 5315HelicalUniRule annotation1 PublicationAdd
BLAST
Topological domaini54 – 629Lumenal1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Reaction center, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Cells grow normally under all light regimes tested; it is dispensable for photoautotrophic growth. The deletion strain is more tolerant to photoinhibition, while isolated PSII complex contains less PsbK and Ycf12 than wild-type and also has reduced oxygen-evolving capacity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6262Photosystem II reaction center protein ZPRO_0000217733Add
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, 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.11 Publications

Protein-protein interaction databases

DIPiDIP-48504N.
STRINGi197221.tsr1967.

Structurei

Secondary structure

1
62
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2726Combined sources
Beta strandi30 – 323Combined sources
Turni34 – 363Combined sources
Helixi37 – 5721Combined sources
Turni58 – 614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50Z/z1-62[»]
2AXTX-ray3.00Z/z1-62[»]
3KZIX-ray3.60Z1-62[»]
4FBYX-ray6.56Z/l1-62[»]
4IXQX-ray5.70Z/z1-62[»]
4IXRX-ray5.90Z/z1-62[»]
4PBUX-ray5.00Z/z1-62[»]
4PJ0X-ray2.44Z/z1-62[»]
4RVYX-ray5.50Z/z1-62[»]
4TNHX-ray4.90Z/z1-62[»]
4TNIX-ray4.60Z/z1-62[»]
4TNJX-ray4.50Z/z1-62[»]
4TNKX-ray5.20Z/z1-62[»]
4V62X-ray2.90AZ/BZ1-62[»]
4V82X-ray3.20AZ/BZ1-62[»]
5E7CX-ray4.50Z/z1-62[»]
ProteinModelPortaliQ8DHJ2.
SMRiQ8DHJ2. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DHJ2.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsbZ family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105ZDH. Bacteria.
ENOG4112722. LUCA.
HOGENOMiHOG000264225.
KOiK02724.
OMAiMTIIFQF.
OrthoDBiEOG6J48VK.

Family and domain databases

Gene3Di1.10.287.740. 1 hit.
HAMAPiMF_00644. PSII_PsbZ.
InterProiIPR002644. PSII_PsbZ.
[Graphical view]
PfamiPF01737. Ycf9. 1 hit.
[Graphical view]
ProDomiPD004770. PSII_PsbZ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03043. PS_II_psbZ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8DHJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTILFQLALA ALVILSFVMV IGVPVAYASP QDWDRSKQLI FLGSGLWIAL
60
VLVVGVLNFF VV
Length:62
Mass (Da):6,764
Last modified:March 1, 2003 - v1
Checksum:i313A629F73715DD8
GO

Mass spectrometryi

Molecular mass is 6798±5 Da from positions 1 - 62. Determined by MALDI. 1 Publication
Molecular mass is 6793 Da from positions 1 - 62. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09519.1.
RefSeqiNP_682757.1. NC_004113.1.
WP_011057802.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09519; BAC09519; BAC09519.
GeneIDi1010256.
KEGGitel:tsr1967.
PATRICi23929338. VBITheElo119873_2057.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09519.1.
RefSeqiNP_682757.1. NC_004113.1.
WP_011057802.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50Z/z1-62[»]
2AXTX-ray3.00Z/z1-62[»]
3KZIX-ray3.60Z1-62[»]
4FBYX-ray6.56Z/l1-62[»]
4IXQX-ray5.70Z/z1-62[»]
4IXRX-ray5.90Z/z1-62[»]
4PBUX-ray5.00Z/z1-62[»]
4PJ0X-ray2.44Z/z1-62[»]
4RVYX-ray5.50Z/z1-62[»]
4TNHX-ray4.90Z/z1-62[»]
4TNIX-ray4.60Z/z1-62[»]
4TNJX-ray4.50Z/z1-62[»]
4TNKX-ray5.20Z/z1-62[»]
4V62X-ray2.90AZ/BZ1-62[»]
4V82X-ray3.20AZ/BZ1-62[»]
5E7CX-ray4.50Z/z1-62[»]
ProteinModelPortaliQ8DHJ2.
SMRiQ8DHJ2. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48504N.
STRINGi197221.tsr1967.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09519; BAC09519; BAC09519.
GeneIDi1010256.
KEGGitel:tsr1967.
PATRICi23929338. VBITheElo119873_2057.

Phylogenomic databases

eggNOGiENOG4105ZDH. Bacteria.
ENOG4112722. LUCA.
HOGENOMiHOG000264225.
KOiK02724.
OMAiMTIIFQF.
OrthoDBiEOG6J48VK.

Miscellaneous databases

EvolutionaryTraceiQ8DHJ2.

Family and domain databases

Gene3Di1.10.287.740. 1 hit.
HAMAPiMF_00644. PSII_PsbZ.
InterProiIPR002644. PSII_PsbZ.
[Graphical view]
PfamiPF01737. Ycf9. 1 hit.
[Graphical view]
ProDomiPD004770. PSII_PsbZ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03043. PS_II_psbZ. 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, COFACTOR, SUBUNIT, 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 1-10, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  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 (3.50 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 (3.00 ANGSTROMS) 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) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOPOLOGY.
    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) 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) IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) 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) 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 nameiPSBZ_THEEB
AccessioniPrimary (citable) accession number: Q8DHJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 91 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.