ID EFR_ARATH Reviewed; 1031 AA.
AC C0LGT6; Q0WWU8; Q8S9I3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase EFR {ECO:0000303|PubMed:16713565};
DE EC=2.7.11.1 {ECO:0000269|PubMed:18158241, ECO:0000269|PubMed:29649442};
DE AltName: Full=Elongation factor Tu receptor {ECO:0000303|PubMed:16713565};
DE Short=EF-Tu receptor {ECO:0000303|PubMed:16713565};
DE Flags: Precursor;
GN Name=EFR {ECO:0000303|PubMed:16713565};
GN OrderedLocusNames=At5g20480 {ECO:0000312|Araport:AT5G20480};
GN ORFNames=F7C8.70 {ECO:0000312|EMBL:AF296833};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 893-1031.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16713565; DOI=10.1016/j.cell.2006.03.037;
RA Zipfel C., Kunze G., Chinchilla D., Caniard A., Jones J.D.G., Boller T.,
RA Felix G.;
RT "Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts
RT Agrobacterium-mediated transformation.";
RL Cell 125:749-760(2006).
RN [7]
RP INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO1, AUTOPHOSPHORYLATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=18158241; DOI=10.1016/j.cub.2007.12.020;
RA Xiang T., Zong N., Zou Y., Wu Y., Zhang J., Xing W., Li Y., Tang X.,
RA Zhu L., Chai J., Zhou J.-M.;
RT "Pseudomonas syringae effector AvrPto blocks innate immunity by targeting
RT receptor kinases.";
RL Curr. Biol. 18:74-80(2008).
RN [8]
RP UBIQUITINATION BY AVRPTOB.
RX PubMed=19062288; DOI=10.1016/j.cub.2008.10.063;
RA Goehre V., Spallek T., Haeweker H., Mersmann S., Mentzel T., Boller T.,
RA de Torres M., Mansfield J.W., Robatzek S.;
RT "Plant pattern-recognition receptor FLS2 is directed for degradation by the
RT bacterial ubiquitin ligase AvrPtoB.";
RL Curr. Biol. 18:1824-1832(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19763087; DOI=10.1038/emboj.2009.263;
RA Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H.,
RA Dong X., Robatzek S., Schulze-Lefert P.;
RT "Receptor quality control in the endoplasmic reticulum for plant innate
RT immunity.";
RL EMBO J. 28:3439-3449(2009).
RN [10]
RP FUNCTION.
RX PubMed=19717464; DOI=10.1073/pnas.0905532106;
RA Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D.,
RA Zipfel C., Jones J.D.;
RT "Specific ER quality control components required for biogenesis of the
RT plant innate immune receptor EFR.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009).
RN [11]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=20410299; DOI=10.1074/jbc.m110.124800;
RA Albert M., Jehle A.K., Mueller K., Eisele C., Lipschis M., Felix G.;
RT "Arabidopsis thaliana pattern recognition receptors for bacterial
RT elongation factor Tu and flagellin can be combined to form functional
RT chimeric receptors.";
RL J. Biol. Chem. 285:19035-19042(2010).
RN [12]
RP 3D-STRUCTURE MODELING, AND MUTAGENESIS OF 76-ILE-SER-77; 81-GLY-GLY-82;
RP 103-ASN--ASP-106; 274-GLY-THR-275; 293-GLU-ARG-294; 298-SER-SER-299;
RP 317-TRP-TRP-318; 347-GLU-TYR-348; 373-SER--PHE-375; 397-GLU--SER-399;
RP 447-HIS--ASN-449; 469-ASP--ASP-473; 564-ASN--SER-568 AND 588-ASN--ASN-590.
RX PubMed=21789174; DOI=10.1371/journal.pone.0021614;
RA Helft L., Reddy V., Chen X., Koller T., Federici L., Fernandez-Recio J.,
RA Gupta R., Bent A.;
RT "LRR conservation mapping to predict functional sites within protein
RT leucine-rich repeat domains.";
RL PLoS ONE 6:E21614-E21614(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH SERK3/BAK1; SERK4/BKK1; SERK1 AND SERK2.
RC STRAIN=cv. Columbia;
RX PubMed=21693696; DOI=10.1105/tpc.111.084301;
RA Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N.,
RA Malinovsky F.G., Tor M., de Vries S., Zipfel C.;
RT "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and
RT BKK1/SERK4 are required for innate immunity to hemibiotrophic and
RT biotrophic pathogens.";
RL Plant Cell 23:2440-2455(2011).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT TYR-836 AND TYR-897, MUTAGENESIS OF TYR-702;
RP TYR-791; TYR-836; ASP-849; TYR-875; TYR-877; TYR-897; TYR-902; TYR-915;
RP TYR-939; TYR-944 AND TYR-979, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP HOPD2.
RX PubMed=24625928; DOI=10.1126/science.1248849;
RA Macho A.P., Schwessinger B., Ntoukakis V., Brutus A., Segonzac C., Roy S.,
RA Kadota Y., Oh M.H., Sklenar J., Derbyshire P., Lozano-Duran R.,
RA Malinovsky F.G., Monaghan J., Menke F.L., Huber S.C., He S.Y., Zipfel C.;
RT "A bacterial tyrosine phosphatase inhibits plant pattern recognition
RT receptor activation.";
RL Science 343:1509-1512(2014).
RN [15]
RP INTERACTION WITH IOS1.
RX PubMed=27317676; DOI=10.1105/tpc.16.00313;
RA Yeh Y.-H., Panzeri D., Kadota Y., Huang Y.-C., Huang P.-Y., Tao C.-N.,
RA Roux M., Chien H.-C., Chin T.-C., Chu P.-W., Zipfel C., Zimmerli L.;
RT "The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent
RT and BAK1-independent pattern-triggered immunity.";
RL Plant Cell 28:1701-1721(2016).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH BIK1.
RC STRAIN=cv. Columbia;
RX PubMed=29649442; DOI=10.1016/j.chom.2018.03.010;
RA Lal N.K., Nagalakshmi U., Hurlburt N.K., Flores R., Bak A., Sone P., Ma X.,
RA Song G., Walley J., Shan L., He P., Casteel C., Fisher A.J.,
RA Dinesh-Kumar S.P.;
RT "The receptor-like cytoplasmic kinase BIK1 localizes to the nucleus and
RT regulates defense hormone expression during plant innate immunity.";
RL Cell Host Microbe 23:485-497.e5(2018).
CC -!- FUNCTION: Constitutes the pattern-recognition receptor (PPR) that
CC determines the specific perception of elongation factor Tu (EF-Tu), a
CC potent elicitor of the defense response to pathogen-associated
CC molecular patterns (PAMPs); phosphorylates BIK1 upon elicitation to
CC regulate immune responses such as defense hormone expression (e.g.
CC jasmonic acid (JA) and salicylic acid (SA)) (PubMed:29649442). Reduces
CC transformation by Rhizobium radiobacter probably by inducing plant
CC defense during the interaction. Binding to the effector AvrPto1 from
CC P.syringae blocks the downstream plant immune response while
CC interaction with hopD2 decreases the phosphorylation level of EFR upon
CC elf18 treatment. Specific endoplasmic reticulum quality control
CC components (ERD2B, CRT3, UGGT and STT3A) are required for the
CC biogenesis of EFR. {ECO:0000269|PubMed:16713565,
CC ECO:0000269|PubMed:19717464, ECO:0000269|PubMed:19763087,
CC ECO:0000269|PubMed:20410299, ECO:0000269|PubMed:21693696,
CC ECO:0000269|PubMed:24625928, ECO:0000269|PubMed:29649442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:18158241, ECO:0000269|PubMed:29649442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18158241,
CC ECO:0000269|PubMed:29649442};
CC -!- SUBUNIT: Binds to Pseudomonas syringae AvrPto1 and (via the kinase and
CC cytoplasmic domains) to hopD2. Interacts with SERK3/BAK1, SERK4/BKK1,
CC SERK1 and SERK2 in a specific ligand-induced manner. Binds to IOS1
CC (PubMed:27317676). Binds to BIK1 in the absence of pathogen elicitor;
CC dissociates upon pathogen-associated molecular pattern (PAMP)-triggered
CC activation (PubMed:29649442). {ECO:0000269|PubMed:18158241,
CC ECO:0000269|PubMed:21693696, ECO:0000269|PubMed:24625928,
CC ECO:0000269|PubMed:27317676, ECO:0000269|PubMed:29649442}.
CC -!- INTERACTION:
CC C0LGT6; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-8801168, EBI-16902452;
CC C0LGT6; Q94F62: BAK1; NbExp=3; IntAct=EBI-8801168, EBI-617138;
CC C0LGT6; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-8801168, EBI-20651739;
CC C0LGT6; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-8801168, EBI-16146189;
CC C0LGT6; Q03250: RBG7; NbExp=4; IntAct=EBI-8801168, EBI-1393626;
CC C0LGT6; Q8LPS5: SERK5; NbExp=4; IntAct=EBI-8801168, EBI-16887868;
CC C0LGT6; Q79LY0: hopD2; Xeno; NbExp=3; IntAct=EBI-8801168, EBI-16096022;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Endomembrane system; Single-pass type I membrane protein.
CC -!- DOMAIN: The last two LRR (561-597) are necessary for elf18 binding and
CC functionality. {ECO:0000269|PubMed:20410299}.
CC -!- PTM: Autophosphorylated after elicitation with elfl18.
CC Autophosphorylation is inhibited by the binding with avrPto1.
CC Phosphorylation at T-836 is required for immune signaling.
CC {ECO:0000269|PubMed:24625928}.
CC -!- PTM: Polyubiquitinated at the kinase domain mediated by P.syringae
CC AvrPtoB. {ECO:0000269|PubMed:19062288}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to R.radiobacter.
CC {ECO:0000269|PubMed:16713565}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92850.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70991.1; -; Genomic_DNA.
DR EMBL; AY075690; AAL77697.1; -; mRNA.
DR EMBL; BT005820; AAO64755.1; -; mRNA.
DR EMBL; FJ708780; ACN59371.1; -; mRNA.
DR EMBL; AK226237; BAE98400.1; -; mRNA.
DR RefSeq; NP_001318610.1; NM_001343669.1.
DR RefSeq; NP_197548.1; NM_122055.5.
DR AlphaFoldDB; C0LGT6; -.
DR SMR; C0LGT6; -.
DR BioGRID; 17446; 23.
DR DIP; DIP-61674N; -.
DR IntAct; C0LGT6; 28.
DR MINT; C0LGT6; -.
DR STRING; 3702.C0LGT6; -.
DR GlyCosmos; C0LGT6; 18 sites, No reported glycans.
DR iPTMnet; C0LGT6; -.
DR PaxDb; 3702-AT5G20480-1; -.
DR ProteomicsDB; 220737; -.
DR EnsemblPlants; AT5G20480.1; AT5G20480.1; AT5G20480.
DR EnsemblPlants; AT5G20480.2; AT5G20480.2; AT5G20480.
DR GeneID; 832170; -.
DR Gramene; AT5G20480.1; AT5G20480.1; AT5G20480.
DR Gramene; AT5G20480.2; AT5G20480.2; AT5G20480.
DR KEGG; ath:AT5G20480; -.
DR Araport; AT5G20480; -.
DR TAIR; AT5G20480; EFR.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR InParanoid; C0LGT6; -.
DR OMA; SYFGNMT; -.
DR OrthoDB; 5477463at2759; -.
DR PhylomeDB; C0LGT6; -.
DR PRO; PR:C0LGT6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGT6; baseline and differential.
DR Genevisible; C0LGT6; AT.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019199; F:transmembrane receptor protein kinase activity; TAS:TAIR.
DR GO; GO:0016045; P:detection of bacterium; IDA:TAIR.
DR GO; GO:0002764; P:immune response-regulating signaling pathway; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0010359; P:regulation of anion channel activity; IMP:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008:SF470; BNAC09G37350D PROTEIN; 1.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1031
FT /note="LRR receptor-like serine/threonine-protein kinase
FT EFR"
FT /id="PRO_0000387508"
FT TOPO_DOM 25..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..1031
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 98..120
FT /note="LRR 1"
FT REPEAT 122..144
FT /note="LRR 2"
FT REPEAT 146..168
FT /note="LRR 3"
FT REPEAT 170..193
FT /note="LRR 4"
FT REPEAT 194..216
FT /note="LRR 5"
FT REPEAT 218..240
FT /note="LRR 6"
FT REPEAT 242..264
FT /note="LRR 7"
FT REPEAT 267..289
FT /note="LRR 8"
FT REPEAT 291..312
FT /note="LRR 9"
FT REPEAT 315..335
FT /note="LRR 10"
FT REPEAT 345..368
FT /note="LRR 11"
FT REPEAT 370..392
FT /note="LRR 12"
FT REPEAT 394..416
FT /note="LRR 13"
FT REPEAT 418..440
FT /note="LRR 14"
FT REPEAT 442..464
FT /note="LRR 15"
FT REPEAT 466..487
FT /note="LRR 16"
FT REPEAT 490..512
FT /note="LRR 17"
FT REPEAT 514..536
FT /note="LRR 18"
FT REPEAT 538..560
FT /note="LRR 19"
FT REPEAT 561..584
FT /note="LRR 20"
FT REPEAT 585..597
FT /note="LRR 21"
FT DOMAIN 712..1001
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1005..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 849
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 718..726
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 741
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 709
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 791
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 836
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:24625928"
FT MOD_RES 897
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:24625928"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 76..77
FT /note="IS->AA: No effect on elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 81..82
FT /note="GG->AA: No effect on elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 103..106
FT /note="NLAD->ALAA: Insensitive to elf18."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 274..275
FT /note="GT->AA: No effect on elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 293..294
FT /note="ER->AA: No effect on elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 298..299
FT /note="SS->AA: No effect on elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 317..318
FT /note="WW->AA: Decreased elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 347..348
FT /note="EY->AA: Decreased elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 373..375
FT /note="SLF->ALA: No effect on elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 397..399
FT /note="ELS->ALA: Decreased elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 447..449
FT /note="HLN->ALA: Insensitive to elf18."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 469..473
FT /note="DLWMD->ALWMA: Insensitive to elf18."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 564..568
FT /note="NVDFS->AVDFA: Decreased elf18 sensitivity."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 588..590
FT /note="NLN->ALA: Insensitive to elf18."
FT /evidence="ECO:0000269|PubMed:21789174"
FT MUTAGEN 702
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 791
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 836
FT /note="Y->F: Loss of elf18-triggered immunity, but no
FT effect on the kinase activity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 849
FT /note="D->N: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 875
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 877
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 897
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 902
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 915
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 939
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 944
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT MUTAGEN 979
FT /note="Y->F: No effect on elf18-triggered immunity."
FT /evidence="ECO:0000269|PubMed:24625928"
FT CONFLICT 893
FT /note="G -> L (in Ref. 5; BAE98400)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="K -> E (in Ref. 3; AAL77697/AAO64755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 113353 MW; E0E0AE671DA9124D CRC64;
MKLSFSLVFN ALTLLLQVCI FAQARFSNET DMQALLEFKS QVSENNKREV LASWNHSSPF
CNWIGVTCGR RRERVISLNL GGFKLTGVIS PSIGNLSFLR LLNLADNSFG STIPQKVGRL
FRLQYLNMSY NLLEGRIPSS LSNCSRLSTV DLSSNHLGHG VPSELGSLSK LAILDLSKNN
LTGNFPASLG NLTSLQKLDF AYNQMRGEIP DEVARLTQMV FFQIALNSFS GGFPPALYNI
SSLESLSLAD NSFSGNLRAD FGYLLPNLRR LLLGTNQFTG AIPKTLANIS SLERFDISSN
YLSGSIPLSF GKLRNLWWLG IRNNSLGNNS SSGLEFIGAV ANCTQLEYLD VGYNRLGGEL
PASIANLSTT LTSLFLGQNL ISGTIPHDIG NLVSLQELSL ETNMLSGELP VSFGKLLNLQ
VVDLYSNAIS GEIPSYFGNM TRLQKLHLNS NSFHGRIPQS LGRCRYLLDL WMDTNRLNGT
IPQEILQIPS LAYIDLSNNF LTGHFPEEVG KLELLVGLGA SYNKLSGKMP QAIGGCLSME
FLFMQGNSFD GAIPDISRLV SLKNVDFSNN NLSGRIPRYL ASLPSLRNLN LSMNKFEGRV
PTTGVFRNAT AVSVFGNTNI CGGVREMQLK PCIVQASPRK RKPLSVRKKV VSGICIGIAS
LLLIIIVASL CWFMKRKKKN NASDGNPSDS TTLGMFHEKV SYEELHSATS RFSSTNLIGS
GNFGNVFKGL LGPENKLVAV KVLNLLKHGA TKSFMAECET FKGIRHRNLV KLITVCSSLD
SEGNDFRALV YEFMPKGSLD MWLQLEDLER VNDHSRSLTP AEKLNIAIDV ASALEYLHVH
CHDPVAHCDI KPSNILLDDD LTAHVSDFGL AQLLYKYDRE SFLNQFSSAG VRGTIGYAAP
EYGMGGQPSI QGDVYSFGIL LLEMFSGKKP TDESFAGDYN LHSYTKSILS GCTSSGGSNA
IDEGLRLVLQ VGIKCSEEYP RDRMRTDEAV RELISIRSKF FSSKTTITES PRDAPQSSPQ
EWMLNTDMHT M
//
