Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Photosystem II reaction center protein H

Gene

psbH

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), required for its stability and/or assembly. 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.UniRule annotation4 Publications

Cofactori

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II reaction center protein HUniRule annotation
Short name:
PSII-HUniRule annotation
Gene namesi
Name:psbHUniRule annotation
Ordered Locus Names:tsl1386
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 3029Cytoplasmic1 PublicationAdd
BLAST
Transmembranei31 – 4414Helical1 PublicationAdd
BLAST
Topological domaini45 – 6622Lumenal1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Not essential for photoautotrophic growth, however PSII is less stable, a considerable amount is missing the oxygen evolving complex, and it is missing PsbX.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 6665Photosystem II reaction center protein HPRO_0000070546Add
BLAST

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-48493N.
STRINGi197221.tsl1386.

Structurei

Secondary structure

1
66
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116Combined sources
Helixi12 – 154Combined sources
Turni24 – 274Combined sources
Helixi28 – 4922Combined sources
Turni56 – 583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50H/h1-66[»]
2AXTX-ray3.00H/h1-66[»]
3KZIX-ray3.60H2-66[»]
4FBYX-ray6.56H/W2-66[»]
4IXQX-ray5.70H/h1-66[»]
4IXRX-ray5.90H/h1-66[»]
4PBUX-ray5.00H/h2-66[»]
4PJ0X-ray2.44H/h1-66[»]
4RVYX-ray5.50H/h2-66[»]
4TNHX-ray4.90H/h1-66[»]
4TNIX-ray4.60H/h1-66[»]
4TNJX-ray4.50H/h1-66[»]
4TNKX-ray5.20H/h1-66[»]
4V62X-ray2.90AH/BH1-66[»]
4V82X-ray3.20AH/BH1-66[»]
5E7CX-ray4.50H/h2-66[»]
ProteinModelPortaliQ8DJ43.
SMRiQ8DJ43. Positions 2-65.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8DJ43.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsbH family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105WIA. Bacteria.
ENOG41123BF. LUCA.
HOGENOMiHOG000246916.
KOiK02709.
OMAiPLMAVFM.
OrthoDBiEOG63NMPF.

Family and domain databases

HAMAPiMF_00752. PSII_PsbH.
InterProiIPR001056. PSII_PsbH.
[Graphical view]
PfamiPF00737. PsbH. 1 hit.
[Graphical view]
ProDomiPD003584. PSII_PsbH. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

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

Q8DJ43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRTWLGDI LRPLNSEYGK VAPGWGTTPL MAVFMGLFLV FLLIILEIYN
60
STLILDGVNV SWKALG
Length:66
Mass (Da):7,354
Last modified:March 1, 2003 - v1
Checksum:iA7558EDCD943741D
GO

Mass spectrometryi

Molecular mass is 7227±5 Da from positions 2 - 66. Determined by MALDI. 1 Publication
Molecular mass is 7223 Da from positions 2 - 66. Determined by MALDI. 1 Publication
Molecular mass is 7178 Da from positions 2 - 66. Determined by MALDI. Missing initiator Met and CO2.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08938.1.
RefSeqiNP_682176.1. NC_004113.1.
WP_011057226.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08938; BAC08938; BAC08938.
GeneIDi1011628.
KEGGitel:tsl1386.
PATRICi23928122. VBITheElo119873_1458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08938.1.
RefSeqiNP_682176.1. NC_004113.1.
WP_011057226.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50H/h1-66[»]
2AXTX-ray3.00H/h1-66[»]
3KZIX-ray3.60H2-66[»]
4FBYX-ray6.56H/W2-66[»]
4IXQX-ray5.70H/h1-66[»]
4IXRX-ray5.90H/h1-66[»]
4PBUX-ray5.00H/h2-66[»]
4PJ0X-ray2.44H/h1-66[»]
4RVYX-ray5.50H/h2-66[»]
4TNHX-ray4.90H/h1-66[»]
4TNIX-ray4.60H/h1-66[»]
4TNJX-ray4.50H/h1-66[»]
4TNKX-ray5.20H/h1-66[»]
4V62X-ray2.90AH/BH1-66[»]
4V82X-ray3.20AH/BH1-66[»]
5E7CX-ray4.50H/h2-66[»]
ProteinModelPortaliQ8DJ43.
SMRiQ8DJ43. Positions 2-65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48493N.
STRINGi197221.tsl1386.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC08938; BAC08938; BAC08938.
GeneIDi1011628.
KEGGitel:tsl1386.
PATRICi23928122. VBITheElo119873_1458.

Phylogenomic databases

eggNOGiENOG4105WIA. Bacteria.
ENOG41123BF. LUCA.
HOGENOMiHOG000246916.
KOiK02709.
OMAiPLMAVFM.
OrthoDBiEOG63NMPF.

Miscellaneous databases

EvolutionaryTraceiQ8DJ43.

Family and domain databases

HAMAPiMF_00752. PSII_PsbH.
InterProiIPR001056. PSII_PsbH.
[Graphical view]
PfamiPF00737. PsbH. 1 hit.
[Graphical view]
ProDomiPD003584. PSII_PsbH. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.
  2. Cited for: PROTEIN SEQUENCE OF 2-8, CLEAVAGE OF INITIATOR METHIONINE, COFACTOR, SUBCELLULAR LOCATION.
  3. "Absence of the psbH gene product destabilizes the Photosystem II complex and prevents association of the Photosystem II-X protein in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
    Iwai M., Katayama M., Ikeuchi M.
    Photosyn. Res. 87:313-322(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: BP-1.
  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) OF 2-66 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) OF 2-66 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 2-66 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 nameiPSBH_THEEB
AccessioniPrimary (citable) accession number: Q8DJ43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 90 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.