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Protein

Photosystem II manganese-stabilizing polypeptide

Gene

psbO

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

Functioni

Part of the oxygen-evolving complex associated with photosystem II (PSII). 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.3 Publications

Cofactori

Note: PSII binds multiple chlorophylls, carotenoids and specific lipids.9 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II manganese-stabilizing polypeptide
Short name:
MSP
Gene namesi
Name:psbO
Ordered Locus Names:tll0444
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 – 26262 PublicationsAdd
BLAST
Chaini27 – 272246Photosystem II manganese-stabilizing polypeptidePRO_0000029567Add
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-48499N.
STRINGi197221.tll0444.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 364Combined sources
Turni37 – 393Combined sources
Helixi41 – 433Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 7916Combined sources
Beta strandi84 – 863Combined sources
Beta strandi91 – 933Combined sources
Beta strandi95 – 984Combined sources
Beta strandi104 – 11310Combined sources
Beta strandi119 – 1279Combined sources
Beta strandi129 – 1357Combined sources
Turni136 – 1383Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi167 – 1759Combined sources
Beta strandi190 – 1967Combined sources
Helixi206 – 2083Combined sources
Helixi209 – 2124Combined sources
Beta strandi218 – 23114Combined sources
Turni232 – 2354Combined sources
Beta strandi236 – 24611Combined sources
Turni250 – 2534Combined sources
Beta strandi258 – 27114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50O/o27-272[»]
2AXTX-ray3.00O/o26-272[»]
3KZIX-ray3.60O27-272[»]
4FBYX-ray6.56O/f27-272[»]
4IXQX-ray5.70O/o1-272[»]
4IXRX-ray5.90O/o1-272[»]
4PBUX-ray5.00O/o30-272[»]
4PJ0X-ray2.44O/o1-272[»]
4RVYX-ray5.50O/o30-272[»]
4TNHX-ray4.90O/o1-272[»]
4TNIX-ray4.60O/o1-272[»]
4TNJX-ray4.50O/o1-272[»]
4TNKX-ray5.20O/o1-272[»]
4V62X-ray2.90AO/BO26-272[»]
4V82X-ray3.20AO/BO26-272[»]
5E7CX-ray4.50O/o30-272[»]
ProteinModelPortaliP0A431.
SMRiP0A431. Positions 27-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A431.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsbO family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CPJ. Bacteria.
ENOG410XP4G. LUCA.
HOGENOMiHOG000232492.
KOiK02716.
OMAiFQPITVL.
OrthoDBiEOG6GBM8H.

Family and domain databases

InterProiIPR011250. OMP/PagP_b-brl.
IPR002628. PSII_MSP.
[Graphical view]
PfamiPF01716. MSP. 1 hit.
[Graphical view]
SUPFAMiSSF56925. SSF56925. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYRILMATL LAVCLGIFSL SAPAFAAKQT LTYDDIVGTG LANKCPTLDD
60 70 80 90 100
TARGAYPIDS SQTYRIARLC LQPTTFLVKE EPKNKRQEAE FVPTKLVTRE
110 120 130 140 150
TTSLDQIQGE LKVNSDGSLT FVEEDGIDFQ PVTVQMAGGE RIPLLFTVKN
160 170 180 190 200
LVASTQPNVT SITTSTDFKG EFNVPSYRTA NFLDPKGRGL ASGYDSAIAL
210 220 230 240 250
PQAKEEELAR ANVKRFSLTK GQISLNVAKV DGRTGEIAGT FESEQLSDDD
260 270
MGAHEPHEVK IQGVFYASIE PA
Length:272
Mass (Da):29,608
Last modified:March 15, 2005 - v1
Checksum:i1F053A3453990141
GO

Mass spectrometryi

Molecular mass is 26830±30 Da from positions 27 - 272. Determined by MALDI. 1 Publication
Molecular mass is 26820 Da from positions 27 - 272. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC07996.1.
RefSeqiNP_681234.1. NC_004113.1.
WP_011056297.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC07996; BAC07996; BAC07996.
GeneIDi1012686.
KEGGitel:tll0444.
PATRICi23926130. VBITheElo119873_0468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC07996.1.
RefSeqiNP_681234.1. NC_004113.1.
WP_011056297.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S5LX-ray3.50O/o27-272[»]
2AXTX-ray3.00O/o26-272[»]
3KZIX-ray3.60O27-272[»]
4FBYX-ray6.56O/f27-272[»]
4IXQX-ray5.70O/o1-272[»]
4IXRX-ray5.90O/o1-272[»]
4PBUX-ray5.00O/o30-272[»]
4PJ0X-ray2.44O/o1-272[»]
4RVYX-ray5.50O/o30-272[»]
4TNHX-ray4.90O/o1-272[»]
4TNIX-ray4.60O/o1-272[»]
4TNJX-ray4.50O/o1-272[»]
4TNKX-ray5.20O/o1-272[»]
4V62X-ray2.90AO/BO26-272[»]
4V82X-ray3.20AO/BO26-272[»]
5E7CX-ray4.50O/o30-272[»]
ProteinModelPortaliP0A431.
SMRiP0A431. Positions 27-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48499N.
STRINGi197221.tll0444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC07996; BAC07996; BAC07996.
GeneIDi1012686.
KEGGitel:tll0444.
PATRICi23926130. VBITheElo119873_0468.

Phylogenomic databases

eggNOGiENOG4105CPJ. Bacteria.
ENOG410XP4G. LUCA.
HOGENOMiHOG000232492.
KOiK02716.
OMAiFQPITVL.
OrthoDBiEOG6GBM8H.

Miscellaneous databases

EvolutionaryTraceiP0A431.

Family and domain databases

InterProiIPR011250. OMP/PagP_b-brl.
IPR002628. PSII_MSP.
[Graphical view]
PfamiPF01716. MSP. 1 hit.
[Graphical view]
SUPFAMiSSF56925. SSF56925. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.
  2. "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 27-272 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  3. "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 26-272 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  4. "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 26-272 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Strain: BP-1.
  5. "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 27-272 IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
    Strain: BP-1.
  6. "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 26-272 IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 27-272 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  9. "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 30-272 IN PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BP-1.

Entry informationi

Entry nameiPSBO_THEEB
AccessioniPrimary (citable) accession number: P0A431
Secondary accession number(s): P55221, Q54074
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: April 13, 2016
This is version 79 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, 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.