PSBK_SPIOL
ID PSBK_SPIOL Reviewed; 59 AA.
AC P12163; Q9M3M8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Photosystem II reaction center protein K {ECO:0000255|HAMAP-Rule:MF_00441};
DE Short=PSII-K {ECO:0000255|HAMAP-Rule:MF_00441};
DE Flags: Precursor;
GN Name=psbK {ECO:0000255|HAMAP-Rule:MF_00441};
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], PROTEIN SEQUENCE OF 23-35, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RA Murata N., Miyao M., Hayashida N., Hidaka T., Sugiura M.;
RT "Identification of a new gene in the chloroplast genome encoding a low-
RT molecular-mass polypeptide of photosystem II complex.";
RL FEBS Lett. 235:283-288(1988).
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 23-34, SUBUNIT, AND SUBCELLULAR LOCATION.
RA Schroeder W.P., Henrysson T., Aakerlund H.-E.;
RT "Characterization of low molecular mass proteins of photosystem II by N-
RT terminal sequencing.";
RL FEBS Lett. 235:289-292(1988).
RN [4]
RP PROTEIN SEQUENCE OF 23-36, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [5]
RP PROTEIN SEQUENCE OF 23-30, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP 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).
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. May
CC be involved in PSII dimerization (PubMed:9632665).
CC {ECO:0000269|PubMed:9632665}.
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:0000255|HAMAP-Rule:MF_00441}.
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. This protein, PsbL and plastoquinone-9 are found in PSII
CC dimers but not seen in PSII monomers (PubMed:9632665).
CC {ECO:0000255|HAMAP-Rule:MF_00441, ECO:0000269|PubMed:2644131,
CC ECO:0000269|PubMed:9632665, ECO:0000269|Ref.1, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00441, ECO:0000269|PubMed:2644131,
CC ECO:0000269|PubMed:9632665, ECO:0000269|Ref.1, ECO:0000269|Ref.3};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00441}.
CC -!- MASS SPECTROMETRY: Mass=4292.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9632665};
CC -!- SIMILARITY: Belongs to the PsbK family. {ECO:0000255|HAMAP-
CC Rule:MF_00441}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA31277.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X12786; CAA31277.2; ALT_INIT; Genomic_DNA.
DR EMBL; AJ400848; CAB88708.1; -; Genomic_DNA.
DR PIR; S01122; S01122.
DR RefSeq; NP_054915.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; K/k=1-59.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P12163; -.
DR SMR; P12163; -.
DR DIP; DIP-62017N; -.
DR IntAct; P12163; 1.
DR STRING; 3562.P12163; -.
DR GeneID; 2715616; -.
DR KEGG; soe:2715616; -.
DR OrthoDB; 1631304at2759; -.
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_00441; PSII_PsbK; 1.
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 3D-structure; Chloroplast; Direct protein sequencing; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Reaction center;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT PROPEP 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00441,
FT ECO:0000269|PubMed:2644131, ECO:0000269|PubMed:9632665,
FT ECO:0000269|Ref.1, ECO:0000269|Ref.3"
FT /id="PRO_0000029529"
FT CHAIN 23..59
FT /note="Photosystem II reaction center protein K"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00441"
FT /id="PRO_0000029530"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00441"
FT CONFLICT 4
FT /note="I -> T (in Ref. 1; CAA31277)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="I -> IGI (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..15
FT /note="ALY -> TLF (in Ref. 1; CAA31277)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> N (in Ref. 1; CAA31277)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="F -> I (in Ref. 1; CAA31277)"
FT /evidence="ECO:0000305"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 41..55
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 59 AA; 6749 MW; 25FCFA8925CE157F CRC64;
MLNIFSLICL NSALYSSSFF FGKLPEAYAF LSPIVDFMPV IPLFFFLLAF VWQAAVSFR
