EFR_ARATH » LRR receptor-like serine/threonine-protein kinase EFR

EFR_ARATH » LRR receptor-like serine/threonine-protein kinase EFR
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
EFR_ARATH » LRR receptor-like serine/threonine-protein kinase EFR » Elongation factor Tu receptor;EF-Tu receptor;
Hydrophobic Thickness 34.4 ± 2.4 Å
Tilt Angle 32 ± 1°
ΔGtransfer -24.5 kcal/mol
ΔGfold -20.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology Out
TM Segments 648-674 (644-678)
Pathways

Plant-pathogen interaction (KEGG)

PDB none
OPM none
Complexes none
Interactions

BAK1, Complex: BAK1:EFR

PERK5, Complex: PERK5:EFR

Domains

AA: 28-69, PDBID: 4MN8, Subunit A, Seq Identity:35%, Leucine rich repeat N-terminal domain

AA: 122-144, PDBID: 3RGX, Subunit A, Seq Identity:48%, Leucine Rich Repeat

AA: 145-205, PDBID: 4MN8, Subunit A, Seq Identity:39%, Leucine rich repeat

AA: 266-326, PDBID: 4M7E, Subunit C, Seq Identity:46%, Leucine rich repeat

AA: 712-992, PDBID: 4OA2, Subunit A, Seq Identity:37%, Protein kinase domain

UniProt annotation for EFR_ARATH » LRR receptor-like serine/threonine-protein kinase EFR
FUNCTION: Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of elongation factor Tu (EF- Tu), a potent elicitor of the defense response to pathogen- associated molecular patterns (PAMPs). Reduces transformation by Rhizobium radiobacter probably by inducing plant defense during the interaction. Binding to the effector AvrPto1 from P.syringae blocks the downstream plant immune response while interaction with hopD2 decreases the phosphorylation level of EFR upon elf18 treatment. Specific endoplasmic reticulum quality control components (ERD2B, CRT3, UGGT and STT3A) are required for the biogenesis of EFR.

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.

SUBUNIT: Binds to Pseudomonas syringae AvrPto1 and (via the kinase and cytoplasmic domains) to hopD2. Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a specific ligand-induced manner.

DOMAIN: The last two LRR (561-597) are necessary for elf18 binding and functionality.

UniProt features for EFR_ARATH » LRR receptor-like serine/threonine-protein kinase EFR
SIGNAL 1 24 Potential.
CHAIN 25 1031 LRR receptor-like serine/threonine- protein kinase EFR.
REPEAT 98 120 LRR 1.
REPEAT 122 144 LRR 2.
REPEAT 146 168 LRR 3.
REPEAT 170 193 LRR 4.
REPEAT 194 216 LRR 5.
REPEAT 218 240 LRR 6.
REPEAT 242 264 LRR 7.
REPEAT 267 289 LRR 8.
REPEAT 291 312 LRR 9.
REPEAT 315 335 LRR 10.
REPEAT 345 368 LRR 11.
REPEAT 370 392 LRR 12.
REPEAT 394 416 LRR 13.
REPEAT 418 440 LRR 14.
REPEAT 442 464 LRR 15.
REPEAT 466 487 LRR 16.
REPEAT 490 512 LRR 17.
REPEAT 514 536 LRR 18.
REPEAT 538 560 LRR 19.
REPEAT 561 584 LRR 20.
REPEAT 585 597 LRR 21.
DOMAIN 712 1001 Protein kinase.
ACT_SITE 849 849 Proton acceptor (By similarity).
Amino Acid Sequence for EFR_ARATH » LRR receptor-like serine/threonine-protein kinase EFR
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