PSB27_THEVB
ID PSB27_THEVB Reviewed; 134 AA.
AC Q8DG60;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Photosystem II lipoprotein Psb27 {ECO:0000255|HAMAP-Rule:MF_01481};
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}; OrderedLocusNames=tll2464;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, CHARACTERIZATION AS A LIPOPROTEIN, SUBUNIT, PROBABLE SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RX PubMed=17114356; DOI=10.1105/tpc.106.042671;
RA Nowaczyk M.M., Hebeler R., Schlodder E., Meyer H.E., Warscheid B.,
RA Rogner M.;
RT "Psb27, a cyanobacterial lipoprotein, is involved in the repair cycle of
RT photosystem II.";
RL Plant Cell 18:3121-3131(2006).
RN [3]
RP CHARACTERIZATION OF PARTIALLY ASSEMBLED PSII.
RX PubMed=17432833; DOI=10.1021/bi7000399;
RA Mamedov F., Nowaczyk M.M., Thapper A., Rogner M., Styring S.;
RT "Functional characterization of monomeric photosystem II core preparations
RT from Thermosynechococcus elongatus with or without the Psb27 protein.";
RL Biochemistry 46:5542-5551(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 24-134.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=22193820; DOI=10.1007/s11120-011-9712-7;
RA Michoux F., Takasaka K., Boehm M., Komenda J., Nixon P.J., Murray J.W.;
RT "Crystal structure of the Psb27 assembly factor at 1.6 A: implications for
RT binding to Photosystem II.";
RL Photosyn. Res. 110:169-175(2012).
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 Its presence in a photosystem II (PSII) preparation prevents binding of
CC other extrinsic subunits PsbO, PsbU and PsbV, and thus assembly of
CC calcium-manganese-oxide cluster. Psb27-containing complexes lack oxygen
CC evolving activity and an oxidizable calcium-manganese-oxide cluster,
CC but have a normal reaction center. {ECO:0000269|PubMed:17114356}.
CC -!- SUBUNIT: Monomer. Forms a complex with a monomeric, partially assembled
CC PSII consisting of D1 (psbA), D2 (psbD), CP47 (psbB), CP43 (psbC) and a
CC number of the small subunits but that does not include PsbO, PsbU or
CC PsbV. This is probably the complex in which D1 is assembled and/or
CC replaced. {ECO:0000269|PubMed:17114356}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305}; Lipid-
CC anchor {ECO:0000305}; Lumenal side {ECO:0000305}. Note=Associated with
CC PSII on the lumenal side of the thylakoid membrane. Might also be
CC associated with the cell's inner membrane.
CC -!- MASS SPECTROMETRY: Mass=13518.1; Method=MALDI; Note=Isolated from
CC PSII.; Evidence={ECO:0000269|PubMed:17114356};
CC -!- MASS SPECTROMETRY: Mass=13252.3; Method=MALDI; Note=After treatment
CC with Lipolase for 5 minutes.; Evidence={ECO:0000269|PubMed:17114356};
CC -!- MASS SPECTROMETRY: Mass=13013.2; Method=MALDI; Note=After treatment
CC with Lipolase for 30 minutes.; Evidence={ECO:0000269|PubMed:17114356};
CC -!- SIMILARITY: Belongs to the Psb27 family. {ECO:0000255|HAMAP-
CC Rule:MF_01481}.
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DR EMBL; BA000039; BAC10015.1; -; Genomic_DNA.
DR RefSeq; NP_683253.1; NC_004113.1.
DR RefSeq; WP_011058295.1; NC_004113.1.
DR PDB; 2Y6X; X-ray; 1.60 A; A=24-134.
DR PDB; 7NHP; EM; 2.72 A; 1=1-134.
DR PDBsum; 2Y6X; -.
DR PDBsum; 7NHP; -.
DR AlphaFoldDB; Q8DG60; -.
DR SMR; Q8DG60; -.
DR STRING; 197221.22296191; -.
DR EnsemblBacteria; BAC10015; BAC10015; BAC10015.
DR KEGG; tel:tll2464; -.
DR PATRIC; fig|197221.4.peg.2588; -.
DR eggNOG; ENOG5031CPI; Bacteria.
DR OMA; HYSSYPN; -.
DR OrthoDB; 1677766at2; -.
DR BRENDA; 1.10.3.9; 7763.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0009523; C:photosystem II; IDA:UniProtKB.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; IDA:UniProtKB.
DR GO; GO:0031977; C:thylakoid lumen; IEA:UniProtKB-UniRule.
DR GO; GO:0010207; P:photosystem II assembly; IDA:UniProtKB.
DR GO; GO:0010206; P:photosystem II repair; IDA: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; Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW Thylakoid.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01481"
FT CHAIN 22..134
FT /note="Photosystem II lipoprotein Psb27"
FT /id="PRO_0000422925"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7NHP"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:2Y6X"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7NHP"
FT HELIX 57..75
FT /evidence="ECO:0007829|PDB:2Y6X"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:2Y6X"
FT HELIX 85..103
FT /evidence="ECO:0007829|PDB:2Y6X"
FT HELIX 111..133
FT /evidence="ECO:0007829|PDB:2Y6X"
SQ SEQUENCE 134 AA; 15100 MW; CC16CEB2D8F7EE24 CRC64;
MKRFWAMVCA LFLSVSLLLT SCANVPTGLT GNFREDTLAL ISSLREAIAL PENDPNKKAA
QAEARKKLND FFALYRRDDS LRSLSSFMTM QTALNSLAGH YSSYPNRPLP EKLKARLEQE
FKQVELALDR EAKS
