PSBO1_ARATH
ID PSBO1_ARATH Reviewed; 332 AA.
AC P23321; O81917; Q41998; Q8L7F1; Q8LAT1; Q93Y28; Q93ZP8; Q94JV7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Oxygen-evolving enhancer protein 1-1, chloroplastic {ECO:0000303|PubMed:2583096};
DE Short=OEE1 {ECO:0000303|PubMed:2583096};
DE AltName: Full=33 kDa subunit of oxygen evolving system of photosystem II {ECO:0000303|PubMed:2101691};
DE AltName: Full=33 kDa thylakoid membrane protein {ECO:0000303|PubMed:2101691};
DE AltName: Full=Manganese-stabilizing protein 1 {ECO:0000303|PubMed:15722336};
DE Short=MSP-1 {ECO:0000303|PubMed:15722336};
DE AltName: Full=OEC 33 kDa subunit {ECO:0000303|PubMed:11826309, ECO:0000303|PubMed:9802567};
DE Flags: Precursor;
GN Name=PSBO1 {ECO:0000303|PubMed:11719511};
GN Synonyms=OEC33 {ECO:0000303|PubMed:11826309},
GN PSBO {ECO:0000303|PubMed:9802567};
GN OrderedLocusNames=At5g66570 {ECO:0000312|Araport:AT5G66570};
GN ORFNames=K1F13.25 {ECO:0000312|EMBL:BAB10933.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2101691; DOI=10.1007/bf00018562;
RA Ko K., Granell A., Bennett J., Cashmore A.R.;
RT "Isolation and characterization of cDNAs from Lycopersicon esculentum and
RT Arabidopsis thaliana encoding the 33 kDa protein of the photosystem II-
RT associated oxygen-evolving complex.";
RL Plant Mol. Biol. 14:217-227(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9802567; DOI=10.1093/dnares/5.4.221;
RA Jain P.K., Kochhar A., Khurana J.P., Tyagi A.K.;
RT "The psbO gene for 33-kDa precursor polypeptide of the oxygen-evolving
RT complex in Arabidopsis thaliana -- nucleotide sequence and control of its
RT expression.";
RL DNA Res. 5:221-228(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-179.
RC STRAIN=cv. C24; TISSUE=Flower bud;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-90, AND SUBCELLULAR LOCATION.
RX PubMed=2583096; DOI=10.1002/j.1460-2075.1989.tb08477.x;
RA Ko K., Cashmore A.R.;
RT "Targeting of proteins to the thylakoid lumen by the bipartite transit
RT peptide of the 33 kd oxygen-evolving protein.";
RL EMBO J. 8:3187-3194(1989).
RN [9]
RP PROTEIN SEQUENCE OF 86-93, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [10]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11826309; DOI=10.1105/tpc.010304;
RA Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G.,
RA Rudella A., Liberles D.A., Soederberg L., Roepstorff P., von Heijne G.,
RA van Wijk K.J.;
RT "Central functions of the lumenal and peripheral thylakoid proteome of
RT Arabidopsis determined by experimentation and genome-wide prediction.";
RL Plant Cell 14:211-236(2002).
RN [11]
RP FUNCTION.
RX PubMed=12123820; DOI=10.1016/s0014-5793(02)02963-0;
RA Murakami R., Ifuku K., Takabayashi A., Shikanai T., Endo T., Sato F.;
RT "Characterization of an Arabidopsis thaliana mutant with impaired psbO, one
RT of two genes encoding extrinsic 33-kDa proteins in photosystem II.";
RL FEBS Lett. 523:138-142(2002).
RN [12]
RP FUNCTION.
RX PubMed=15722336; DOI=10.1074/jbc.m501550200;
RA Yi X., McChargue M., Laborde S., Frankel L.K., Bricker T.M.;
RT "The manganese-stabilizing protein is required for photosystem II
RT assembly/stability and photoautotrophy in higher plants.";
RL J. Biol. Chem. 280:16170-16174(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [14]
RP INTERACTION WITH CV.
RC STRAIN=cv. Columbia;
RX PubMed=25538186; DOI=10.1105/tpc.114.133116;
RA Wang S., Blumwald E.;
RT "Stress-induced chloroplast degradation in Arabidopsis is regulated via a
RT process independent of autophagy and senescence-associated vacuoles.";
RL Plant Cell 26:4875-4888(2014).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.30 ANGSTROMS) OF 86-332.
RX PubMed=28604725; DOI=10.1038/nplants.2017.80;
RA van Bezouwen L.S., Caffarri S., Kale R.S., Kouril R., Thunnissen A.W.H.,
RA Oostergetel G.T., Boekema E.J.;
RT "Subunit and chlorophyll organization of the plant photosystem II
RT supercomplex.";
RL Nat. Plants 3:17080-17080(2017).
CC -!- FUNCTION: Stabilizes the manganese cluster which is the primary site of
CC water splitting. {ECO:0000269|PubMed:12123820,
CC ECO:0000269|PubMed:15722336}.
CC -!- SUBUNIT: Interacts with CV in the chloroplast thylakoid membrane and in
CC CV-containing vesicles (CCVs). {ECO:0000269|PubMed:25538186}.
CC -!- INTERACTION:
CC P23321; P0AA25: trxA; Xeno; NbExp=2; IntAct=EBI-449414, EBI-368542;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:2583096}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:2583096}; Lumenal side
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:2583096}.
CC Note=Associated with the photosystem II complex.
CC -!- TISSUE SPECIFICITY: Leaves.
CC -!- MISCELLANEOUS: PSBO1 is the major isoform in the wild-type and it
CC cannot be fully complemented by PSBO2.
CC -!- SIMILARITY: Belongs to the PsbO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA79171.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X52428; CAA36675.1; -; mRNA.
DR EMBL; Y15433; CAA75629.1; -; Genomic_DNA.
DR EMBL; AB013389; BAB10933.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98230.1; -; Genomic_DNA.
DR EMBL; AF424626; AAL11619.1; -; mRNA.
DR EMBL; AY052299; AAK96492.1; -; mRNA.
DR EMBL; AY061924; AAL31251.1; -; mRNA.
DR EMBL; AF372898; AAK49614.1; -; mRNA.
DR EMBL; AY136291; AAM96957.1; -; mRNA.
DR EMBL; AY054583; AAK96774.1; -; mRNA.
DR EMBL; AY056401; AAL08257.1; -; mRNA.
DR EMBL; BT000407; AAN15726.1; -; mRNA.
DR EMBL; AY087630; AAM65169.1; -; mRNA.
DR EMBL; Z18374; CAA79171.1; ALT_FRAME; mRNA.
DR PIR; S11852; S11852.
DR RefSeq; NP_201458.1; NM_126055.4.
DR PDB; 5MDX; EM; 5.30 A; O/o=86-332.
DR PDB; 7OUI; EM; 2.79 A; O/o=86-332.
DR PDBsum; 5MDX; -.
DR PDBsum; 7OUI; -.
DR AlphaFoldDB; P23321; -.
DR SMR; P23321; -.
DR BioGRID; 22031; 3.
DR IntAct; P23321; 8.
DR MINT; P23321; -.
DR STRING; 3702.AT5G66570.1; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; P23321; -.
DR SWISS-2DPAGE; P23321; -.
DR PaxDb; P23321; -.
DR PRIDE; P23321; -.
DR ProteomicsDB; 226229; -.
DR DNASU; 836789; -.
DR EnsemblPlants; AT5G66570.1; AT5G66570.1; AT5G66570.
DR GeneID; 836789; -.
DR Gramene; AT5G66570.1; AT5G66570.1; AT5G66570.
DR KEGG; ath:AT5G66570; -.
DR Araport; AT5G66570; -.
DR TAIR; locus:2154940; AT5G66570.
DR eggNOG; ENOG502QRXA; Eukaryota.
DR HOGENOM; CLU_063138_0_0_1; -.
DR InParanoid; P23321; -.
DR OMA; FAHKCVD; -.
DR OrthoDB; 924219at2759; -.
DR PhylomeDB; P23321; -.
DR BioCyc; MetaCyc:AT5G66570-MON; -.
DR PRO; PR:P23321; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P23321; baseline and differential.
DR Genevisible; P23321; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; ISS:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0055035; C:plastid thylakoid membrane; IDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0010242; F:oxygen evolving activity; IDA:TAIR.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
DR GO; GO:0019684; P:photosynthesis, light reaction; IDA:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
DR GO; GO:0042549; P:photosystem II stabilization; IMP:TAIR.
DR GO; GO:0035304; P:regulation of protein dephosphorylation; IMP:TAIR.
DR DisProt; DP02577; -.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR002628; PSII_MSP.
DR PANTHER; PTHR34058; PTHR34058; 1.
DR Pfam; PF01716; MSP; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Manganese; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11826309"
FT TRANSIT 59..85
FT /note="Thylakoid"
FT CHAIN 86..332
FT /note="Oxygen-evolving enhancer protein 1-1, chloroplastic"
FT /id="PRO_0000029553"
FT CONFLICT 57
FT /note="D -> N (in Ref. 5; AAN15726/AAM96957)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> S (in Ref. 5; AAL08257)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..114
FT /note="QC -> HS (in Ref. 1; CAA36675)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="A -> S (in Ref. 6; AAM65169)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="G -> C (in Ref. 5; AAK96774)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="T -> S (in Ref. 5; AAK49614)"
FT /evidence="ECO:0000305"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:7OUI"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 132..146
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 282..293
FT /evidence="ECO:0007829|PDB:7OUI"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:7OUI"
FT STRAND 320..331
FT /evidence="ECO:0007829|PDB:7OUI"
SQ SEQUENCE 332 AA; 35142 MW; 73174DDC09C11E5C CRC64;
MAASLQSTAT FLQSAKIATA PSRGSSHLRS TQAVGKSFGL ETSSARLTCS FQSDFKDFTG
KCSDAVKIAG FALATSALVV SGASAEGAPK RLTYDEIQSK TYMEVKGTGT ANQCPTIDGG
SETFSFKPGK YAGKKFCFEP TSFTVKADSV SKNAPPEFQN TKLMTRLTYT LDEIEGPFEV
ASDGSVNFKE EDGIDYAAVT VQLPGGERVP FLFTVKQLDA SGKPDSFTGK FLVPSYRGSS
FLDPKGRGGS TGYDNAVALP AGGRGDEEEL VKENVKNTAA SVGEITLKVT KSKPETGEVI
GVFESLQPSD TDLGAKVPKD VKIQGVWYGQ LE
