FLS2_ARATH » LRR receptor-like serine/threonine-protein kinase FLS2

FLS2_ARATH » LRR receptor-like serine/threonine-protein kinase FLS2
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
FLS2_ARATH » LRR receptor-like serine/threonine-protein kinase FLS2 » Protein FLAGELLIN-SENSING 2;Protein FLAGELLIN-SENSITIVE 2;
Hydrophobic Thickness 39.2 ± 2.0 Å
Tilt Angle 5 ± 5°
ΔGtransfer -60.0 kcal/mol
ΔGfold -27.5 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology Out
TM Segments 804-832 (800-836)
Pathways

Plant-pathogen interaction (KEGG)

PDB 4mna (25-800), 4mn8 (A=25-800)
OPM none
Complexes

BAK1:FLS2_ARATH

Interactions

BAK1, Complex: FLS2:BAK1, PDBID: 4mn8, PubMed

P2C70, Complex: P2C70:FLS2, PubMed

PAM74, Complex: FLS2:PAM74

Domains

AA: 28-69, PDBID: 4MN8, Subunit A, Seq Identity:100%, Leucine rich repeat N-terminal domain

AA: 217-239, PDBID: 4MN8, Subunit A, Seq Identity:100%, Leucine Rich Repeat

AA: 673-734, PDBID: 4MN8, Subunit A, Seq Identity:100%, Leucine rich repeat

AA: 702-758, PDBID: 4MN8, Subunit A, Seq Identity:100%, Leucine rich repeat

AA: 870-1154, PDBID: 3TL8, Subunit A, Seq Identity:37%, Protein kinase domain

UniProt annotation for FLS2_ARATH » LRR receptor-like serine/threonine-protein kinase FLS2
FUNCTION: Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 or to the phosphatase hopD2 from Pseudomonas syringae blocks the downstream plant immune response.

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

SUBUNIT: Interacts with KAPP. Interacts with BAK1. Does not form homodimer. Interacts with SERK3/BAK1, SERK4/BKK1, SERK1 and SERK2 in a specific ligand-induced manner. Interacts with P.syringae AvrPto1, AvrPtoB and (via the kinase and cytoplasmic domains) hopD2. Interacts with PBS1.

TISSUE SPECIFICITY: Ubiquitously expressed.

INDUCTION: Repressed upon infection with the P.syringae virulent DC3000 strain, in a flg22- and avrPtoB-dependent manner (at protein level).

DOMAIN: Both extracellular leucine-rich repeats and protein kinase domains are required for flg22-binding. The LRR 9 to LRR 15 domains are involved in flg22-binding.

MISCELLANEOUS: After flg22-binding, forms instantaneously a heteromeric complex with BAK1 and is transphosphorylated within 15 seconds. After activation, the receptor is internalized by endocytosis and subject to degradation.

UniProt features for FLS2_ARATH » LRR receptor-like serine/threonine-protein kinase FLS2
SIGNAL 1 23 Potential.
CHAIN 24 1173 LRR receptor-like serine/threonine- protein kinase FLS2.
REPEAT 97 119 LRR 1.
REPEAT 121 143 LRR 2.
REPEAT 145 167 LRR 3.
REPEAT 169 192 LRR 4.
REPEAT 193 215 LRR 5.
REPEAT 217 240 LRR 6.
REPEAT 241 263 LRR 7.
REPEAT 265 288 LRR 8.
REPEAT 289 311 LRR 9.
REPEAT 313 335 LRR 10.
REPEAT 337 359 LRR 11.
REPEAT 361 383 LRR 12.
REPEAT 385 407 LRR 13.
REPEAT 409 431 LRR 14.
REPEAT 432 454 LRR 15.
REPEAT 456 478 LRR 16.
REPEAT 480 503 LRR 17.
REPEAT 504 527 LRR 18.
REPEAT 528 550 LRR 19.
REPEAT 552 574 LRR 20.
REPEAT 576 599 LRR 21.
REPEAT 600 621 LRR 22.
REPEAT 627 649 LRR 23.
REPEAT 650 673 LRR 24.
REPEAT 674 696 LRR 25.
REPEAT 699 721 LRR 26.
REPEAT 723 746 LRR 27.
REPEAT 747 769 LRR 28.
DOMAIN 870 1155 Protein kinase.
ACT_SITE 997 997 Proton acceptor (By similarity).
Amino Acid Sequence for FLS2_ARATH » LRR receptor-like serine/threonine-protein kinase FLS2
MKLLSKTFLI LTLTFFFFGI ALAKQSFEPE IEALKSFKNG ISNDPLGVLS DWTIIGSLRH CNWTGITCDS TGHVVSVSLL EKQLEGVLSP AIANLTYLQV LDLTSNSFTG KIPAEIGKLT ELNQLILYLN YFSGSIPSGI WELKNIFYLD LRNNLLSGDV PEEICKTSSL VLIGFDYNNL TGKIPECLGD LVHLQMFVAA GNHLTGSIPV SIGTLANLTD LDLSGNQLTG KIPRDFGNLL NLQSLVLTEN LLEGDIPAEI GNCSSLVQLE LYDNQLTGKI PAELGNLVQL QALRIYKNKL TSSIPSSLFR LTQLTHLGLS ENHLVGPISE EIGFLESLEV LTLHSNNFTG EFPQSITNLR NLTVLTVGFN NISGELPADL GLLTNLRNLS AHDNLLTGPI PSSISNCTGL KLLDLSHNQM TGEIPRGFGR MNLTFISIGR NHFTGEIPDD IFNCSNLETL SVADNNLTGT LKPLIGKLQK LRILQVSYNS LTGPIPREIG NLKDLNILYL HSNGFTGRIP REMSNLTLLQ GLRMYSNDLE GPIPEEMFDM KLLSVLDLSN NKFSGQIPAL FSKLESLTYL SLQGNKFNGS IPASLKSLSL LNTFDISDNL LTGTIPGELL ASLKNMQLYL NFSNNLLTGT IPKELGKLEM VQEIDLSNNL FSGSIPRSLQ ACKNVFTLDF SQNNLSGHIP DEVFQGMDMI ISLNLSRNSF SGEIPQSFGN MTHLVSLDLS SNNLTGEIPE SLANLSTLKH LKLASNNLKG HVPESGVFKN INASDLMGNT DLCGSKKPLK PCTIKQKSSH FSKRTRVILI ILGSAAALLL VLLLVLILTC CKKKEKKIEN SSESSLPDLD SALKLKRFEP KELEQATDSF NSANIIGSSS LSTVYKGQLE DGTVIAVKVL NLKEFSAESD KWFYTEAKTL SQLKHRNLVK ILGFAWESGK TKALVLPFME NGNLEDTIHG SAAPIGSLLE KIDLCVHIAS GIDYLHSGYG FPIVHCDLKP ANILLDSDRV AHVSDFGTAR ILGFREDGST TASTSAFEGT IGYLAPEFAY MRKVTTKADV FSFGIIMMEL MTKQRPTSLN DEDSQDMTLR QLVEKSIGNG RKGMVRVLDM ELGDSIVSLK QEEAIEDFLK LCLFCTSSRP EDRPDMNEIL THLMKLRGKA NSFREDRNED REV