ID   PSBL_ANEMR              Reviewed;          38 AA.
AC   B0YPP4;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 43.
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   Aneura mirabilis (Parasitic liverwort) (Cryptothallus mirabilis).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura.
OX   NCBI_TaxID=280810;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18056074; DOI=10.1093/molbev/msm267;
RA   Wickett N.J., Zhang Y., Hansen S.K., Roper J.M., Kuehl J.V., Plock S.A.,
RA   Wolf P.G., dePamphilis C.W., Boore J.L., Goffinet B.;
RT   "Functional gene losses occur with minimal size reduction in the plastid
RT   genome of the parasitic liverwort Aneura mirabilis.";
RL   Mol. Biol. Evol. 25:393-401(2008).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01317}.
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 membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01317}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01317}.
CC   -!- SIMILARITY: Belongs to the PsbL family. {ECO:0000255|HAMAP-
CC       Rule:MF_01317}.
CC   -!- CAUTION: This organism being non-photosynthetic, the role of this
CC       protein is uncertain. {ECO:0000305}.
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DR   EMBL; EU043314; ABS54491.1; -; Genomic_DNA.
DR   RefSeq; YP_001687230.1; NC_010359.1.
DR   AlphaFoldDB; B0YPP4; -.
DR   SMR; B0YPP4; -.
DR   GeneID; 5952216; -.
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:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042651; C:thylakoid membrane; 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   3: Inferred from homology;
KW   Membrane; Photosynthesis; Photosystem II; Plastid; Reaction center;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..38
FT                   /note="Photosystem II reaction center protein L"
FT                   /id="PRO_0000353250"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01317"
SQ   SEQUENCE   38 AA;  4453 MW;  1C73781163D39D7F CRC64;
     MTQPNPNKQS VELNRTSLYW GLLLIFVLAV SFSNYFFN