ID   PSBK_PEA                Reviewed;          46 AA.
AC   P28642; Q9T2J7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 3.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Photosystem II reaction center protein K {ECO:0000303|PubMed:1807835};
DE            Short=PSII-K;
DE   Flags: Precursor; Fragment;
GN   Name=psbK {ECO:0000303|PubMed:1807835};
OS   Pisum sativum (Garden pea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC   STRAIN=cv. Alaska;
RX   PubMed=1807835; DOI=10.1007/bf00317074;
RA   Nagano Y., Matsuno R., Sasaki Y.;
RT   "Sequence and transcriptional analysis of the gene cluster trnQ-zfpA-psaI-
RT   ORF231-petA in pea chloroplasts.";
RL   Curr. Genet. 20:431-436(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-32, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS 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   [3]
RP   PROTEIN SEQUENCE OF 25-46.
RX   PubMed=8262226; DOI=10.1016/0014-5793(93)81617-9;
RA   Zakharov S.D., Ewy R.G., Dilley R.A.;
RT   "Subunit III of the chloroplast ATP-synthase can form a Ca(2+)-binding site
RT   on the lumenal side of the thylakoid membrane.";
RL   FEBS Lett. 336:95-99(1993).
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.
CC       {ECO:0000250|UniProtKB:Q9F1K9}.
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:0000269|PubMed:8262226, ECO:0000269|PubMed:9632665}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:8262226, ECO:0000269|PubMed:9632665}; Single-pass
CC       membrane protein {ECO:0000250|UniProtKB:Q9F1K9}.
CC   -!- SIMILARITY: Belongs to the PsbK family. {ECO:0000305}.
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DR   EMBL; X56315; CAA39753.1; -; Genomic_DNA.
DR   PIR; S17919; S17919.
DR   AlphaFoldDB; P28642; -.
DR   SMR; P28642; -.
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-KW.
DR   InterPro; IPR003687; PSII_PsbK.
DR   InterPro; IPR037270; PSII_PsbK_sf.
DR   PANTHER; PTHR35325; PTHR35325; 1.
DR   Pfam; PF02533; PsbK; 1.
DR   SUPFAM; SSF161037; SSF161037; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Membrane; Photosynthesis;
KW   Photosystem II; Plastid; Reaction center; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..24
FT                   /evidence="ECO:0000269|PubMed:8262226,
FT                   ECO:0000269|PubMed:9632665"
FT                   /id="PRO_0000029505"
FT   CHAIN           25..46
FT                   /note="Photosystem II reaction center protein K"
FT                   /id="PRO_0000029506"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        31
FT                   /note="A -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         46
SQ   SEQUENCE   46 AA;  5126 MW;  382B64B0C5417633 CRC64;
     MLNIFSLVCI CINSALYSSS FFLGKLPEAY AFLNPIVDFM PVIPLL