PSBL_SYNY3
ID PSBL_SYNY3 Reviewed; 39 AA.
AC Q55354;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Photosystem II reaction center protein L {ECO:0000255|HAMAP-Rule:MF_01317};
DE Short=PSII-L {ECO:0000255|HAMAP-Rule:MF_01317};
GN Name=psbL {ECO:0000255|HAMAP-Rule:MF_01317}; OrderedLocusNames=smr0007;
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].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=2116128; DOI=10.1515/znc-1990-0519;
RA Pakrasi H.B., Nyhus K.J., Granok H.;
RT "Targeted deletion mutagenesis of the beta subunit of cytochrome b559
RT protein destabilizes the reaction center of photosystem II.";
RL Z. Naturforsch. C 45:423-429(1990).
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 1-20, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-16; TYR-20;
RP 24-LEU-LEU-25; PHE-33; 36-TYR--ASN-39; TYR-36; PHE-37; PHE-38 AND ASN-39.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18953669; DOI=10.1007/s11120-008-9375-1;
RA Luo H., Eaton-Rye J.J.;
RT "Directed mutagenesis of the transmembrane domain of the PsbL subunit of
RT photosystem II in Synechocystis sp. PCC 6803.";
RL Photosyn. Res. 98:337-347(2008).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 6-ASN--ASN-8; 11-PRO-VAL-12 AND
RP 13-GLU--ASN-15.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=24576450; DOI=10.1016/j.bbabio.2014.02.015;
RA Luo H., Jackson S.A., Fagerlund R.D., Summerfield T.C., Eaton-Rye J.J.;
RT "The importance of the hydrophilic region of PsbL for the plastoquinone
RT electron acceptor complex of Photosystem II.";
RL Biochim. Biophys. Acta 1837:1435-1446(2014).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that
CC uses light energy to abstract electrons from H(2)O, generating O(2) and
CC a proton gradient subsequently used for ATP formation. It consists of a
CC core antenna complex that captures photons, and an electron transfer
CC chain that converts photonic excitation into a charge separation. This
CC subunit is found at the monomer-monomer interface and is required for
CC correct PSII assembly and/or dimerization (By similarity). Required for
CC PSII activity, at least in part due to its effects on PSII assembly.
CC May make specific contact(s) with lipids. {ECO:0000255|HAMAP-
CC Rule:MF_01317, ECO:0000269|PubMed:18834146,
CC ECO:0000269|PubMed:2116128}.
CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_01317,
CC ECO:0000269|PubMed:12069591}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01317, ECO:0000269|PubMed:12069591}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01317}.
CC -!- DISRUPTION PHENOTYPE: Very poor to no photoautotrophic growth, no O(2)
CC evolution. No assembly of PSII monomers or dimers; the CP43-less
CC monomeric intermediate is assembled. {ECO:0000269|PubMed:18834146,
CC ECO:0000269|PubMed:18953669}.
CC -!- SIMILARITY: Belongs to the PsbL family. {ECO:0000255|HAMAP-
CC Rule:MF_01317}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M33897; AAA27301.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17094.1; -; Genomic_DNA.
DR PIR; S75180; S75180.
DR PDB; 6WJ6; EM; 2.58 A; L=1-39.
DR PDB; 7N8O; EM; 1.93 A; L/l=1-39.
DR PDB; 7RCV; EM; 2.01 A; L/l=1-39.
DR PDBsum; 6WJ6; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; Q55354; -.
DR SMR; Q55354; -.
DR IntAct; Q55354; 2.
DR STRING; 1148.1652170; -.
DR PaxDb; Q55354; -.
DR EnsemblBacteria; BAA17094; BAA17094; BAA17094.
DR KEGG; syn:smr0007; -.
DR eggNOG; ENOG5033AKP; Bacteria.
DR InParanoid; Q55354; -.
DR BioCyc; MetaCyc:PSBL-MON; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
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:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01317; PSII_PsbL; 1.
DR InterPro; IPR003372; PSII_PsbL.
DR InterPro; IPR037266; PSII_PsbL_sf.
DR Pfam; PF02419; PsbL; 1.
DR SUPFAM; SSF161017; SSF161017; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Photosynthesis;
KW Photosystem II; Reaction center; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..39
FT /note="Photosystem II reaction center protein L"
FT /id="PRO_0000219795"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01317"
FT MUTAGEN 6..8
FT /note="Missing: Grows like wild-type, increased sensitivity
FT to high light."
FT /evidence="ECO:0000269|PubMed:24576450"
FT MUTAGEN 11..12
FT /note="Missing: Grows like wild-type, decreased dimer
FT formation, increased sensitivity to high light."
FT /evidence="ECO:0000269|PubMed:24576450"
FT MUTAGEN 13..15
FT /note="Missing: Severely impairs photoautotrophic growth,
FT 3-fold less PSII assembles, decreased dimer formation,
FT increased sensitivity to high light with incomplete
FT recovery (increased susceptibility to photodamage)."
FT /evidence="ECO:0000269|PubMed:24576450"
FT MUTAGEN 16
FT /note="R->A,E: Grows significantly slower than wild-type,
FT 88% O(2) evolved, increased sensitivity to high light, 90%
FT dimeric PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 16
FT /note="R->K: Behaves like wild-type."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 20
FT /note="Y->A: Grows slightly slower than wild-type,
FT increased sensitivity to high light with incomplete
FT recovery (increased susceptibility to photodamage), 80%
FT dimeric PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 24..25
FT /note="LL->AA: Grows slightly slower than wild-type,
FT increased sensitivity to high light, 90% dimeric PSII
FT assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 33
FT /note="F->A: Grows slightly slower than wild-type, 80% O(2)
FT evolved, increased sensitivity to high light, 90% dimeric
FT PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 36..39
FT /note="Missing: No photoautotrophic growth, accumulates
FT CP43-less monomeric PSII complexes."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 36
FT /note="Y->A: Grows slightly slower than wild-type, 90%
FT dimeric PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 36
FT /note="Y->F: Grows slightly slower than wild-type."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 37
FT /note="F->A: Grows slightly slower than wild-type; 85% O(2)
FT evolved, increased sensitivity to high light, 60% dimeric
FT PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 38
FT /note="F->A: Grows slightly slower than wild-type; 73% O(2)
FT evolved, increased sensitivity to high light, 60% dimeric
FT PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT MUTAGEN 39
FT /note="N->A: Grows slightly slower than wild-type, 80%
FT dimeric PSII assembled."
FT /evidence="ECO:0000269|PubMed:18953669"
FT HELIX 16..38
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 39 AA; 4473 MW; 324EF5FEF5CD490A CRC64;
MDRNSNPNRQ PVELNRTSLY LGLLLVAVLG ILFSSYFFN
