PSBO_PINST
ID PSBO_PINST Reviewed; 116 AA.
AC P84718;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Putative oxygen-evolving enhancer protein 1;
DE Short=OEE1;
DE AltName: Full=33 kDa subunit of oxygen evolving system of photosystem II;
DE AltName: Full=33 kDa thylakoid membrane protein;
DE AltName: Full=OEC 33 kDa subunit;
DE AltName: Full=PS2;
DE Flags: Fragments;
GN Name=PSBO {ECO:0000250|UniProtKB:P26320};
OS Pinus strobus (Eastern white pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Strobus.
OX NCBI_TaxID=3348;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Leaf {ECO:0000269|PubMed:16529377};
RX PubMed=16529377; DOI=10.1094/mpmi-19-0150;
RA Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
RA Witthuhn B.A., David A.J., Gillman J.H.;
RT "Proteomic comparison of needles from blister rust-resistant and
RT susceptible Pinus strobus seedlings reveals upregulation of putative
RT disease resistance proteins.";
RL Mol. Plant Microbe Interact. 19:150-160(2006).
RN [2]
RP CONTAMINATING SEQUENCE.
RX PubMed=23895828; DOI=10.1016/j.jprot.2013.07.009;
RA Nawrot R., Barylski J., Schulze W.X.;
RT "Incorrectly annotated keratin derived peptide sequences lead to misleading
RT MS/MS data interpretation.";
RL J. Proteomics 91:270-273(2013).
CC -!- FUNCTION: Stabilizes the manganese cluster which is the primary site of
CC water splitting. {ECO:0000250|UniProtKB:P23321}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane.
CC Note=Associated with the photosystem II complex.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.7,
CC its MW is: 35.1 kDa. {ECO:0000269|PubMed:16529377}.
CC -!- SIMILARITY: Belongs to the PsbO family. {ECO:0000305}.
CC -!- CAUTION: The order of the peptides shown is unknown.
CC {ECO:0000269|PubMed:16529377}.
CC -!- CAUTION: This sequence was originally thought to contain an additional
CC peptide (PubMed:16529377). However, it was later shown that the peptide
CC is likely to be human type II keratin, a common contaminant in
CC proteomic analyses, so it has been removed and the remaining sequence
CC may also contain further contaminations (PubMed:23895828).
CC {ECO:0000305|PubMed:23895828}.
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DR AlphaFoldDB; P84718; -.
DR PRIDE; P84718; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Manganese; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Thylakoid.
FT CHAIN <1..>116
FT /note="Putative oxygen-evolving enhancer protein 1"
FT /id="PRO_0000240623"
FT NON_CONS 17..18
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 34..35
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 42..43
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 60..61
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 70..71
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 81..82
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 92..93
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_CONS 103..104
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:16529377"
FT NON_TER 116
FT /evidence="ECO:0000303|PubMed:16529377"
SQ SEQUENCE 116 AA; 12277 MW; 765CD68D51B2C9FB CRC64;
DGIDYAAVTV QLPGGERGGS TGYDNAVALP AGGRGSSMLD PKELGQMNIV FEGVSKSYHD
AVALVLPSLK ASTYYEESLY KVINTWADII NRALTEAVAA EAAAAEDPEM ETMYTK