PSBL_SPIOL
ID PSBL_SPIOL Reviewed; 38 AA.
AC P60150; O47030; P12166; P12167; Q34007;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 73.
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};
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING OF INITIATOR CODON.
RC STRAIN=cv. Matador; TISSUE=Leaf;
RX PubMed=8355656; DOI=10.1007/bf00277062;
RA Bock R., Hagemann R., Koessel H., Kudla J.;
RT "Tissue- and stage-specific modulation of RNA editing of the psbF and psbL
RT transcript from spinach plastids -- a new regulatory mechanism?";
RL Mol. Gen. Genet. 240:238-244(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-4, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RX PubMed=9632665; DOI=10.1074/jbc.273.26.16122;
RA Zheleva D., Sharma J., Panico M., Morris H.R., Barber J.;
RT "Isolation and characterization of monomeric and dimeric CP47-reaction
RT center photosystem II complexes.";
RL J. Biol. Chem. 273:16122-16127(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RA Hermann R.G., Alt J., Schiller B., Widger W.R., Cramer W.A.;
RT "Nucleotide sequence of the gene for apocytochrome b-559 on the spinach
RT plastid chromosome: implications for the structure of the membrane
RT protein.";
RL FEBS Lett. 176:239-244(1984).
RN [5]
RP PROTEIN SEQUENCE OF 2-16.
RX PubMed=2644131; DOI=10.1016/0014-5793(89)80482-x;
RA Ikeuchi M., Takio K., Inoue Y.;
RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. 5 and
RT 4.1 kDa components of the O2-evolving core complex from higher plants.";
RL FEBS Lett. 242:263-269(1989).
RN [6]
RP FUNCTION.
RX PubMed=7957890; DOI=10.1016/0014-5793(94)01089-7;
RA Kitamura K., Ozawa S., Shiina T., Toyoshima Y.;
RT "L protein, encoded by psbL, restores normal functioning of the primary
RT quinone acceptor, QA, in isolated D1/D2/CP47/Cytb-559/I photosystem II
RT reaction center core complex.";
RL FEBS Lett. 354:113-116(1994).
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). Probably
CC involved in PSII assembly (PubMed:7957890). May be involved in PSII
CC dimerization (PubMed:9632665). {ECO:0000255|HAMAP-Rule:MF_01317,
CC ECO:0000269|PubMed:7957890, ECO:0000269|PubMed:9632665}.
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000255|HAMAP-Rule:MF_01317}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01317, ECO:0000269|PubMed:9632665}; Single-
CC pass membrane protein {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01317}.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:8355656};
CC Note=The initiator methionine is created by RNA editing.;
CC -!- MASS SPECTROMETRY: Mass=4365.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9632665};
CC -!- SIMILARITY: Belongs to the PsbL family. {ECO:0000255|HAMAP-
CC Rule:MF_01317}.
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DR EMBL; X70699; CAA50030.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ400848; CAB91048.1; -; Genomic_DNA.
DR EMBL; M35673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S31821; S31821.
DR RefSeq; NP_077749.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; L/l=1-38.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P60150; -.
DR SMR; P60150; -.
DR DIP; DIP-62018N; -.
DR IntAct; P60150; 1.
DR STRING; 3562.P60150; -.
DR GeneID; 2715617; -.
DR KEGG; soe:2715617; -.
DR OrthoDB; 1638606at2759; -.
DR Proteomes; UP000054095; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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; Chloroplast; Direct protein sequencing; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Reaction center;
KW Reference proteome; RNA editing; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2644131,
FT ECO:0000269|PubMed:9632665"
FT CHAIN 2..38
FT /note="Photosystem II reaction center protein L"
FT /id="PRO_0000219773"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01317"
FT HELIX 15..37
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 38 AA; 4497 MW; 55537AEC50D25E8D CRC64;
MTQSNPNEQN VELNRTSLYW GLLLIFVLAV LFSNYFFN
