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Protein

Photosystem II lipoprotein Psb27

Gene

psb27

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the repair and/or biogenesis of the calcium-manganese-oxide cluster on the lumenal face of the thylakoid membrane. Photosystem II (PSII) complexes containing this protein are monomeric, are assembly intermediates lacking the calcium-manganese-oxide cluster and miss some of the lumenal subunits. Probably blocks binding of some of the small lumenal subunits.5 Publications

GO - Biological processi

  • photosystem II assembly Source: UniProtKB
  • photosystem II repair Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem II lipoprotein Psb271 PublicationUniRule annotation
Alternative name(s):
Photosystem II 11 kDa proteinUniRule annotation
Gene namesi
Name:psb271 PublicationUniRule annotation
Ordered Locus Names:slr1645
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  • plasma membrane-derived thylakoid photosystem II Source: UniProtKB
  • thylakoid lumen Source: UniProtKB-HAMAP
  • thylakoid membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem II, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Not essential for photoautotrophic growth, under CaCl2 limiting-conditions absolutely required. Impaired recovery after photoinhibition due to impaired assembly of the calcium-manganese-oxide cluster, especially at high light intensities. CP43 (psbC) is more susceptible to degradation, higher turnover of D1 (psbA). Calcium-manganese-oxide cluster assembly is improved in a double psbO-psb27 mutant. A double psbM-psb27 mutant is incapable of photoautotrophic growth, but does assemble the CP43-less assembly intermediate.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 134110Photosystem II lipoprotein Psb27PRO_0000029369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi25 – 251N-palmitoyl cysteineCurated
Lipidationi25 – 251S-diacylglycerol cysteineUniRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Monomer. Forms a complex with a monomeric, partially assembled PSII. This is probably the complex in which D1 is assembled and/or replaced. Present in 6-10% of PSII complexes; mostly in monomeric PSII. These PSII do not evolve oxygen, do not have an assembled calcium-manganese-oxide cluster. Psb27-containing PSII seem to be assembly intermediates; a wild-type strain includes the intrinsic membrane proteins, Psb27, Pbs28, substoichiometric amounts of PsbO and PsbQ but no PsbU or PsbV, while a ctpA deletion mutant includes the intrinsic membrane proteins (D1 as precursor), Psb27, a very low amount of PsbO and PsbQ, but no PsbU or PsbV. Small amounts of Psb27 interact with the lumenal domain of CP43 (psbC) in wild-type and a ctpA mutant. A small amount can also be detected in monomeric and trimeric photosystem I (PSI), possibly via association with PsaB.UniRule annotation3 Publications

Protein-protein interaction databases

IntActiP74367. 7 interactions.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 5117Combined sources
Helixi59 – 7618Combined sources
Helixi78 – 814Combined sources
Beta strandi83 – 853Combined sources
Helixi87 – 10620Combined sources
Helixi113 – 13220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KMFNMR-A25-134[»]
2KNDNMR-A25-134[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP74367.

Family & Domainsi

Sequence similaritiesi

Belongs to the Psb27 family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000232641.
InParanoidiP74367.
KOiK08902.
OMAiGDFAKDT.
OrthoDBiEOG6QVRKK.
PhylomeDBiP74367.

Family and domain databases

HAMAPiMF_01481. PSII_Psb27.
InterProiIPR025585. PSII_Pbs27.
IPR017488. PSII_Psb27_bac.
[Graphical view]
PfamiPF13326. PSII_Pbs27. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03044. PS_II_psb27. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P74367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFLKNQLSR LLALILVVAI GLTACDSGTG LTGNYSQDTL TVIATLREAI
60 70 80 90 100
DLPQDAPNRQ EVQDTARGQI NDYISRYRRK GDAGGLKSFT TMQTALNSLA
110 120 130
GYYTSYGARP IPEKLKKRLQ LEFTQAERSI ERGV
Length:134
Mass (Da):14,786
Last modified:May 30, 2000 - v2
Checksum:iF55F38705209A015
GO

Sequence cautioni

The sequence BAA18462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82936 Genomic DNA. Translation: BAA11640.1.
BA000022 Genomic DNA. Translation: BAA18462.1. Different initiation.
PIRiS76203.

Genome annotation databases

EnsemblBacteriaiBAA18462; BAA18462; BAA18462.
KEGGisyn:slr1645.
PATRICi23841050. VBISynSp132158_2078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82936 Genomic DNA. Translation: BAA11640.1.
BA000022 Genomic DNA. Translation: BAA18462.1. Different initiation.
PIRiS76203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KMFNMR-A25-134[»]
2KNDNMR-A25-134[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP74367. 7 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA18462; BAA18462; BAA18462.
KEGGisyn:slr1645.
PATRICi23841050. VBISynSp132158_2078.

Phylogenomic databases

HOGENOMiHOG000232641.
InParanoidiP74367.
KOiK08902.
OMAiGDFAKDT.
OrthoDBiEOG6QVRKK.
PhylomeDBiP74367.

Miscellaneous databases

EvolutionaryTraceiP74367.

Family and domain databases

HAMAPiMF_01481. PSII_Psb27.
InterProiIPR025585. PSII_Pbs27.
IPR017488. PSII_Psb27_bac.
[Graphical view]
PfamiPF13326. PSII_Pbs27. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03044. PS_II_psb27. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of genes for the 11 kDa and 13 kDa proteins of photosystem II from Synechocystis sp. PCC 6803."
    Ikeuchi M., Katoh H.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  3. "Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates."
    Liu H., Huang R.Y., Chen J., Gross M.L., Pakrasi H.B.
    Proc. Natl. Acad. Sci. U.S.A. 108:18536-18541(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 79-87, FUNCTION, INTERACTION WITH PSBC.
    Strain: PCC 6803 / Kazusa.
  4. "Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides."
    Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K., Pakrasi H.B.
    Biochemistry 41:8004-8012(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, GENE NAME, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: PCC 6803 / Kazusa.
  5. "Evidence that D1 processing is required for manganese binding and extrinsic protein assembly into photosystem II."
    Roose J.L., Pakrasi H.B.
    J. Biol. Chem. 279:45417-45422(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: PCC 6803 / Kazusa.
  6. "Effects of inactivating psbM and psbT on photodamage and assembly of photosystem II in Synechocystis sp. PCC 6803."
    Bentley F.K., Luo H., Dilbeck P., Burnap R.L., Eaton-Rye J.J.
    Biochemistry 47:11637-11646(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: PCC 6803 / Kazusa.
  7. "The Psb27 protein facilitates manganese cluster assembly in photosystem II."
    Roose J.L., Pakrasi H.B.
    J. Biol. Chem. 283:4044-4050(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: PCC 6803 / Kazusa.
  8. "A genetically tagged Psb27 protein allows purification of two consecutive photosystem II (PSII) assembly intermediates in Synechocystis 6803, a cyanobacterium."
    Liu H., Roose J.L., Cameron J.C., Pakrasi H.B.
    J. Biol. Chem. 286:24865-24871(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    Strain: PCC 6803 / Kazusa.
  9. "The Psb27 assembly factor binds to the CP43 complex of photosystem II in the cyanobacterium Synechocystis sp. PCC 6803."
    Komenda J., Knoppova J., Kopecna J., Sobotka R., Halada P., Yu J., Nickelsen J., Boehm M., Nixon P.J.
    Plant Physiol. 158:476-486(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PSBC, CHARACTERIZATION AS A LIPOPROTEIN, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: PCC 6803 / Kazusa.
  10. "Structure of Psb27 in solution: implications for transient binding to photosystem II during biogenesis and repair."
    Cormann K.U., Bangert J.A., Ikeuchi M., Rogner M., Stoll R., Nowaczyk M.M.
    Biochemistry 48:8768-8770(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-134.
    Strain: PCC 6803 / Kazusa.
  11. "Solution structure of Psb27 from cyanobacterial photosystem II."
    Mabbitt P.D., Rautureau G.J., Day C.L., Wilbanks S.M., Eaton-Rye J.J., Hinds M.G.
    Biochemistry 48:8771-8773(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-134.
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiPSB27_SYNY3
AccessioniPrimary (citable) accession number: P74367
Secondary accession number(s): Q55355
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: March 16, 2016
This is version 91 of the entry and version 2 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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.