PSB27_SYNY3
ID PSB27_SYNY3 Reviewed; 134 AA.
AC P74367; Q55355;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Photosystem II lipoprotein Psb27 {ECO:0000255|HAMAP-Rule:MF_01481, ECO:0000303|PubMed:12069591};
DE AltName: Full=Photosystem II 11 kDa protein {ECO:0000255|HAMAP-Rule:MF_01481};
DE Flags: Precursor;
GN Name=psb27 {ECO:0000255|HAMAP-Rule:MF_01481, ECO:0000303|PubMed:12069591};
GN OrderedLocusNames=slr1645;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ikeuchi M., Katoh H.;
RT "Cloning of genes for the 11 kDa and 13 kDa proteins of photosystem II from
RT Synechocystis sp. PCC 6803.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 79-87, FUNCTION, AND INTERACTION WITH PSBC.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=22031695; DOI=10.1073/pnas.1111597108;
RA Liu H., Huang R.Y., Chen J., Gross M.L., Pakrasi H.B.;
RT "Psb27, a transiently associated protein, binds to the chlorophyll binding
RT protein CP43 in photosystem II assembly intermediates.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18536-18541(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, GENE NAME, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15308630; DOI=10.1074/jbc.m408458200;
RA Roose J.L., Pakrasi H.B.;
RT "Evidence that D1 processing is required for manganese binding and
RT extrinsic protein assembly into photosystem II.";
RL J. Biol. Chem. 279:45417-45422(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18834146; DOI=10.1021/bi800804h;
RA Bentley F.K., Luo H., Dilbeck P., Burnap R.L., Eaton-Rye J.J.;
RT "Effects of inactivating psbM and psbT on photodamage and assembly of
RT photosystem II in Synechocystis sp. PCC 6803.";
RL Biochemistry 47:11637-11646(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18089572; DOI=10.1074/jbc.m708960200;
RA Roose J.L., Pakrasi H.B.;
RT "The Psb27 protein facilitates manganese cluster assembly in photosystem
RT II.";
RL J. Biol. Chem. 283:4044-4050(2008).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=21592967; DOI=10.1074/jbc.m111.246231;
RA Liu H., Roose J.L., Cameron J.C., Pakrasi H.B.;
RT "A genetically tagged Psb27 protein allows purification of two consecutive
RT photosystem II (PSII) assembly intermediates in Synechocystis 6803, a
RT cyanobacterium.";
RL J. Biol. Chem. 286:24865-24871(2011).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH PSBC, CHARACTERIZATION AS A
RP LIPOPROTEIN, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=22086423; DOI=10.1104/pp.111.184184;
RA Komenda J., Knoppova J., Kopecna J., Sobotka R., Halada P., Yu J.,
RA Nickelsen J., Boehm M., Nixon P.J.;
RT "The Psb27 assembly factor binds to the CP43 complex of photosystem II in
RT the cyanobacterium Synechocystis sp. PCC 6803.";
RL Plant Physiol. 158:476-486(2012).
RN [10]
RP STRUCTURE BY NMR OF 25-134.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19697957; DOI=10.1021/bi9012726;
RA Cormann K.U., Bangert J.A., Ikeuchi M., Rogner M., Stoll R., Nowaczyk M.M.;
RT "Structure of Psb27 in solution: implications for transient binding to
RT photosystem II during biogenesis and repair.";
RL Biochemistry 48:8768-8770(2009).
RN [11]
RP STRUCTURE BY NMR OF 25-134.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19697958; DOI=10.1021/bi901309c;
RA Mabbitt P.D., Rautureau G.J., Day C.L., Wilbanks S.M., Eaton-Rye J.J.,
RA Hinds M.G.;
RT "Solution structure of Psb27 from cyanobacterial photosystem II.";
RL Biochemistry 48:8771-8773(2009).
CC -!- FUNCTION: Plays a role in the repair and/or biogenesis of the calcium-
CC manganese-oxide cluster on the lumenal face of the thylakoid membrane.
CC Photosystem II (PSII) complexes containing this protein are monomeric,
CC are assembly intermediates lacking the calcium-manganese-oxide cluster
CC and miss some of the lumenal subunits. Probably blocks binding of some
CC of the small lumenal subunits. {ECO:0000269|PubMed:18089572,
CC ECO:0000269|PubMed:18834146, ECO:0000269|PubMed:21592967,
CC ECO:0000269|PubMed:22031695, ECO:0000269|PubMed:22086423}.
CC -!- SUBUNIT: Monomer. Forms a complex with a monomeric, partially assembled
CC PSII. This is probably the complex in which D1 is assembled and/or
CC replaced. Present in 6-10% of PSII complexes; mostly in monomeric PSII.
CC These PSII do not evolve oxygen, do not have an assembled calcium-
CC manganese-oxide cluster. Psb27-containing PSII seem to be assembly
CC intermediates; a wild-type strain includes the intrinsic membrane
CC proteins, Psb27, Pbs28, substoichiometric amounts of PsbO and PsbQ but
CC no PsbU or PsbV, while a ctpA deletion mutant includes the intrinsic
CC membrane proteins (D1 as precursor), Psb27, a very low amount of PsbO
CC and PsbQ, but no PsbU or PsbV. Small amounts of Psb27 interact with the
CC lumenal domain of CP43 (psbC) in wild-type and a ctpA mutant. A small
CC amount can also be detected in monomeric and trimeric photosystem I
CC (PSI), possibly via association with PsaB. {ECO:0000255|HAMAP-
CC Rule:MF_01481, ECO:0000269|PubMed:12069591,
CC ECO:0000269|PubMed:21592967, ECO:0000269|PubMed:22086423}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01481, ECO:0000269|PubMed:15308630,
CC ECO:0000269|PubMed:21592967, ECO:0000269|PubMed:22086423}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_01481, ECO:0000269|PubMed:15308630,
CC ECO:0000269|PubMed:21592967, ECO:0000269|PubMed:22086423}; Lumenal side
CC {ECO:0000255|HAMAP-Rule:MF_01481, ECO:0000269|PubMed:15308630,
CC ECO:0000269|PubMed:21592967, ECO:0000269|PubMed:22086423}.
CC Note=Associated with PSII on the lumenal side of the thylakoid
CC membrane.
CC -!- DISRUPTION PHENOTYPE: Not essential for photoautotrophic growth, under
CC CaCl(2) limiting-conditions absolutely required. Impaired recovery
CC after photoinhibition due to impaired assembly of the calcium-
CC manganese-oxide cluster, especially at high light intensities. CP43
CC (psbC) is more susceptible to degradation, higher turnover of D1
CC (psbA). Calcium-manganese-oxide cluster assembly is improved in a
CC double psbO-psb27 mutant. A double psbM-psb27 mutant is incapable of
CC photoautotrophic growth, but does assemble the CP43-less assembly
CC intermediate. {ECO:0000269|PubMed:18089572,
CC ECO:0000269|PubMed:18834146, ECO:0000269|PubMed:22086423}.
CC -!- SIMILARITY: Belongs to the Psb27 family. {ECO:0000255|HAMAP-
CC Rule:MF_01481}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18462.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D82936; BAA11640.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18462.1; ALT_INIT; Genomic_DNA.
DR PIR; S76203; S76203.
DR PDB; 2KMF; NMR; -; A=25-134.
DR PDB; 2KND; NMR; -; A=25-134.
DR PDBsum; 2KMF; -.
DR PDBsum; 2KND; -.
DR AlphaFoldDB; P74367; -.
DR BMRB; P74367; -.
DR SMR; P74367; -.
DR IntAct; P74367; 7.
DR STRING; 1148.1653549; -.
DR PaxDb; P74367; -.
DR EnsemblBacteria; BAA18462; BAA18462; BAA18462.
DR KEGG; syn:slr1645; -.
DR eggNOG; ENOG5031CPI; Bacteria.
DR InParanoid; P74367; -.
DR OMA; HYSSYPN; -.
DR PhylomeDB; P74367; -.
DR EvolutionaryTrace; P74367; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
DR GO; GO:0031977; C:thylakoid lumen; IEA:UniProtKB-UniRule.
DR GO; GO:0010207; P:photosystem II assembly; IMP:UniProtKB.
DR GO; GO:0010206; P:photosystem II repair; IMP:UniProtKB.
DR Gene3D; 1.20.58.810; -; 1.
DR HAMAP; MF_01481; PSII_Psb27; 1.
DR InterPro; IPR025585; PSII_Pbs27.
DR InterPro; IPR038450; PSII_Pbs27_sf.
DR InterPro; IPR017488; PSII_Psb27_cyano_bac.
DR PANTHER; PTHR34041; PTHR34041; 1.
DR Pfam; PF13326; PSII_Pbs27; 1.
DR TIGRFAMs; TIGR03044; PS_II_psb27; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Photosynthesis; Photosystem II; Reference proteome; Signal; Thylakoid.
FT SIGNAL 1..24
FT CHAIN 25..134
FT /note="Photosystem II lipoprotein Psb27"
FT /id="PRO_0000029369"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01481"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:2KMF"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:2KMF"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2KMF"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2KMF"
FT HELIX 87..106
FT /evidence="ECO:0007829|PDB:2KMF"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:2KMF"
SQ SEQUENCE 134 AA; 14786 MW; F55F38705209A015 CRC64;
MSFLKNQLSR LLALILVVAI GLTACDSGTG LTGNYSQDTL TVIATLREAI DLPQDAPNRQ
EVQDTARGQI NDYISRYRRK GDAGGLKSFT TMQTALNSLA GYYTSYGARP IPEKLKKRLQ
LEFTQAERSI ERGV
