ID   PSBY_SPIOL              Reviewed;         199 AA.
AC   P80470;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Photosystem II core complex proteins psbY, chloroplastic;
DE   AltName: Full=L-arginine-metabolizing enzyme;
DE            Short=L-AME;
DE   Contains:
DE     RecName: Full=Photosystem II protein psbY-1, chloroplastic;
DE     AltName: Full=psbY-A1;
DE   Contains:
DE     RecName: Full=Photosystem II protein psbY-2, chloroplastic;
DE     AltName: Full=psbY-A2;
DE   Flags: Precursor;
GN   Name=PSBY;
OS   Spinacia oleracea (Spinach).
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 [MRNA], AND PROTEIN SEQUENCE OF 86-128 AND 155-179.
RX   PubMed=9829828; DOI=10.1007/s004380050870;
RA   Gau A.E., Thole H.H., Sokolenko A., Altschmied L., Herrmann R.G.,
RA   Pistorius E.K.;
RT   "PsbY, a novel manganese-binding, low-molecular-mass protein associated
RT   with photosystem II.";
RL   Mol. Gen. Genet. 260:56-68(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 86-128, AND CHARACTERIZATION.
RA   Gau A.E., Thole H.H., Pistorius E.K.;
RT   "Isolation and partial characterization of a manganese requiring L-arginine
RT   metabolizing enzyme being present in photosystem II complexes of spinach
RT   and tobacco.";
RL   Z. Naturforsch. C 50:638-651(1995).
CC   -!- FUNCTION: PSBY-1 and -2 are manganese-binding polypeptides with L-
CC       arginine metabolizing enzyme activity. They are a component of the core
CC       of photosystem II. They have also a minor catalase-like activity since
CC       they cause evolution of oxygen from hydrogen peroxide in a reaction
CC       stimulated by manganese.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC       pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Leaves. Not present in stems and roots.
CC   -!- DEVELOPMENTAL STAGE: Developmentally regulated.
CC   -!- INDUCTION: Photocontrolled. Steady-state concentrations increase for
CC       the first 3 hours of illumination and then decline.
CC   -!- MISCELLANEOUS: The central hydrophobic segment does not form a
CC       membrane-spanning region but could serve as a targeting signal for
CC       processing of the precursor in the thylakoid membrane.
CC   -!- SIMILARITY: Belongs to the PsbY family. {ECO:0000305}.
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DR   EMBL; AF060198; AAC95000.1; -; mRNA.
DR   PIR; T08902; T08902.
DR   AlphaFoldDB; P80470; -.
DR   SMR; P80470; -.
DR   BRENDA; 1.97.1.12; 5812.
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:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00717; PSII_PsbY; 2.
DR   InterPro; IPR038760; PsbY_plant.
DR   InterPro; IPR009388; PSII_PsbY.
DR   PANTHER; PTHR34790; PTHR34790; 1.
DR   Pfam; PF06298; PsbY; 2.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Manganese; Membrane;
KW   Photosynthesis; Photosystem II; Plastid; Repeat; Thylakoid;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..85
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:9829828, ECO:0000269|Ref.2"
FT   CHAIN           86..128
FT                   /note="Photosystem II protein psbY-1, chloroplastic"
FT                   /id="PRO_0000029613"
FT   PROPEP          129..154
FT                   /evidence="ECO:0000269|PubMed:9829828"
FT                   /id="PRO_0000029614"
FT   CHAIN           155..199
FT                   /note="Photosystem II protein psbY-2, chloroplastic"
FT                   /id="PRO_0000029615"
FT   TOPO_DOM        86..94
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..129
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..199
FT                   /note="Stromal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   199 AA;  20664 MW;  0808D5EFB2808C86 CRC64;
     MAATMATTMA VLNTKCLTLN TNKTTSTSPK PTSKPISLSP LGLSNSKLPM GLSPIITAPA
     IAGAVFATLG SVDPAFAVQQ LADIAAEAGT SDNRGLALLL PIIPALGWVL FNILQPALNQ
     INKMRNEKKA FIVGLGLSGL ATSGLLLATP EAQAASEEIA RGSDNRGTLL LLVVLPAIGW
     VLFNILQPAL NQLNKMRSQ