EPS1_ARATH
ID EPS1_ARATH Reviewed; 434 AA.
AC Q9FH97; Q93Y30;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein ENHANCED PSEUDOMONAS SUSCEPTIBILITY 1 {ECO:0000303|PubMed:19036031};
DE EC=2.3.1.- {ECO:0000305};
GN Name=EPS1 {ECO:0000303|PubMed:19036031};
GN OrderedLocusNames=At5g67160 {ECO:0000312|Araport:AT5G67160};
GN ORFNames=K21H1.12 {ECO:0000312|EMBL:BAB10950.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY PATHOGENIC BACTERIA AND
RP JASMONIC ACID.
RC STRAIN=cv. Columbia, and cv. No-0;
RX PubMed=19036031; DOI=10.1111/j.1365-313x.2008.03747.x;
RA Zheng Z., Qualley A., Fan B., Dudareva N., Chen Z.;
RT "An important role of a BAHD acyl transferase-like protein in plant innate
RT immunity.";
RL Plant J. 57:1040-1053(2009).
RN [6]
RP REVIEW.
RX PubMed=19816125; DOI=10.4161/psb.4.6.8392;
RA Chen Z., Zheng Z., Huang J., Lai Z., Fan B.;
RT "Biosynthesis of salicylic acid in plants.";
RL Plant Signal. Behav. 4:493-496(2009).
CC -!- FUNCTION: Required for pathogen-induced salicylic acid (SA)
CC accumulation and SA-mediated resistance to virulent and avirulent
CC pathogens (e.g. P.syringae). {ECO:0000269|PubMed:19036031}.
CC -!- INDUCTION: By pathogenic bacteria (e.g. P.syringae) and jasmonic acid
CC (MeJA). {ECO:0000269|PubMed:19036031}.
CC -!- DISRUPTION PHENOTYPE: Hypersusceptiblity to both virulent and avirulent
CC strains of the bacterial pathogen P.syringae associated with impaired
CC pathogen-mediated induction of salicylic acid (SA) and reduced
CC pathogenesis-related (PR) genes induction. These phenotypes are
CC reversed by SA treatment. In the cv. No-0 but not the cv. Columbia
CC background, defects in SA accumulation or signaling enhances resistance
CC to necrotrophic pathogens such as the fungi B.cinerea and
CC A.brassicicola, leading to small necrotic spots and minor chlorosis, as
CC well as reduced fungal growth. {ECO:0000269|PubMed:19036031}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AB020742; BAB10950.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98308.1; -; Genomic_DNA.
DR EMBL; AY054556; AAK96747.1; -; mRNA.
DR EMBL; AY064619; AAL47333.1; -; mRNA.
DR EMBL; AY087209; AAM64765.1; -; mRNA.
DR RefSeq; NP_201517.1; NM_126116.2.
DR PDB; 6WAO; X-ray; 1.76 A; A/B=1-434.
DR PDB; 6WCS; X-ray; 1.87 A; A/B=1-434.
DR PDBsum; 6WAO; -.
DR PDBsum; 6WCS; -.
DR AlphaFoldDB; Q9FH97; -.
DR SMR; Q9FH97; -.
DR STRING; 3702.AT5G67160.1; -.
DR PaxDb; Q9FH97; -.
DR PRIDE; Q9FH97; -.
DR ProteomicsDB; 230054; -.
DR EnsemblPlants; AT5G67160.1; AT5G67160.1; AT5G67160.
DR GeneID; 836851; -.
DR Gramene; AT5G67160.1; AT5G67160.1; AT5G67160.
DR KEGG; ath:AT5G67160; -.
DR Araport; AT5G67160; -.
DR TAIR; locus:2155573; AT5G67160.
DR eggNOG; ENOG502QVP8; Eukaryota.
DR HOGENOM; CLU_014546_3_0_1; -.
DR InParanoid; Q9FH97; -.
DR OMA; ETHCRLP; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9FH97; -.
DR BioCyc; ARA:AT5G67160-MON; -.
DR BioCyc; MetaCyc:AT5G67160-MON; -.
DR PRO; PR:Q9FH97; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH97; baseline and differential.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IDA:UniProtKB.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IMP:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Plant defense; Reference proteome;
KW Transferase.
FT CHAIN 1..434
FT /note="Protein ENHANCED PSEUDOMONAS SUSCEPTIBILITY 1"
FT /id="PRO_0000439873"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CONFLICT 243
FT /note="A -> T (in Ref. 3; AAK96747/AAL47333)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6WAO"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6WAO"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6WCS"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 255..269
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:6WAO"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 337..349
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:6WAO"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:6WAO"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6WCS"
SQ SEQUENCE 434 AA; 48636 MW; 7E4C4C61DA1624AA CRC64;
MEEELVVISK SIVNPRSLKK PTSVKKIQLT PWDLSRLRFG YLQRGLLFHK IEVKQLQASL
SVALDRFYPL AGRLVKLKND DDTVSFFISC DGSGVEFVHA VAKNIELSDV LELSGSVPGF
FASFFPATGI KNYHGVSRSL LMVQVTEMKD GVFIGFGYNS TVADATSIWK FINAWSEICS
KDSSGSQTFQ RRLHLKGWFF DEIDYPIHIP DPETKPTSYV TTPTNLQEKM FHVTKENVLK
LDAKANDEAD QKISSIQAVL AYIWRSMVKH SGMSREEETH CRLPINMRQR LNPPLEEECF
GNVSQTGIAT VTVGELLDHG LGWAAMQINN MELSQTDEKA KAFAENWVKN IKIPVSVGSK
DLVVTNSHRF DVYCNDFGWG KPIAARAGPP YLNGRLVVFK GIGEASLDFQ ACLLPQVVEK
LVKDAEFNEY VSIV
