SABP2_TOBAC
ID SABP2_TOBAC Reviewed; 260 AA.
AC Q6RYA0; A0A1S3ZW27;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Salicylic acid-binding protein 2 {ECO:0000303|PubMed:14673096};
DE Short=NtSABP2 {ECO:0000303|PubMed:14673096};
DE EC=3.1.1.- {ECO:0000269|PubMed:15668381, ECO:0000269|PubMed:20797615};
DE AltName: Full=Methyl salicylate esterase {ECO:0000303|PubMed:17916738};
GN Name=SABP2 {ECO:0000303|PubMed:14673096}; OrderedLocusNames=LOC107791137;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Xanthi NC;
RX PubMed=14673096; DOI=10.1073/pnas.0307162100;
RA Kumar D., Klessig D.F.;
RT "High-affinity salicylic acid-binding protein 2 is required for plant
RT innate immunity and has salicylic acid-stimulated lipase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:16101-16106(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [3]
RP FUNCTION, MUTAGENESIS OF ALA-13; SER-81 AND HIS-238, AND ACTIVE SITE.
RX PubMed=17916738; DOI=10.1126/science.1147113;
RA Park S.W., Kaimoyo E., Kumar D., Mosher S., Klessig D.F.;
RT "Methyl salicylate is a critical mobile signal for plant systemic acquired
RT resistance.";
RL Science 318:113-116(2007).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=19131332; DOI=10.1074/jbc.m807968200;
RA Park S.W., Liu P.P., Forouhar F., Vlot A.C., Tong L., Tietjen K.,
RA Klessig D.F.;
RT "Use of a synthetic salicylic acid analog to investigate the roles of
RT methyl salicylate and its esterases in plant disease resistance.";
RL J. Biol. Chem. 284:7307-7317(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-12 AND MET-239.
RX PubMed=20797615; DOI=10.1016/j.chembiol.2010.06.013;
RA Padhi S.K., Fujii R., Legatt G.A., Fossum S.L., Berchtold R.,
RA Kazlauskas R.J.;
RT "Switching from an esterase to a hydroxynitrile lyase mechanism requires
RT only two amino acid substitutions.";
RL Chem. Biol. 17:863-871(2010).
RN [6]
RP FUNCTION.
RX PubMed=20621100; DOI=10.1016/j.febslet.2010.06.046;
RA Tripathi D., Jiang Y.L., Kumar D.;
RT "SABP2, a methyl salicylate esterase is required for the systemic acquired
RT resistance induced by acibenzolar-S-methyl in plants.";
RL FEBS Lett. 584:3458-3463(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SALICYLIC ACID,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, MUTAGENESIS OF SER-81, ACTIVE SITE, AND PATHWAY.
RX PubMed=15668381; DOI=10.1073/pnas.0409227102;
RA Forouhar F., Yang Y., Kumar D., Chen Y., Fridman E., Park S.W., Chiang Y.,
RA Acton T.B., Montelione G.T., Pichersky E., Klessig D.F., Tong L.;
RT "Structural and biochemical studies identify tobacco SABP2 as a methyl
RT salicylate esterase and implicate it in plant innate immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1773-1778(2005).
CC -!- FUNCTION: Required to convert methyl salicylate (MeSA) to salicylic
CC acid (SA) as part of the signal transduction pathways that activate
CC systemic acquired resistance in systemic tissue. MeSA is believed to be
CC an inactive form that needs to be demethylated to exert a biological
CC effect. Also able to catalyze the conversion of acibenzolar-S-methyl
CC into acibenzolar to induce systemic acquired resistance.
CC {ECO:0000269|PubMed:14673096, ECO:0000269|PubMed:15668381,
CC ECO:0000269|PubMed:17916738, ECO:0000269|PubMed:19131332,
CC ECO:0000269|PubMed:20621100, ECO:0000269|PubMed:20797615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methyl salicylate = H(+) + methanol + salicylate;
CC Xref=Rhea:RHEA:33611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17790, ChEBI:CHEBI:30762, ChEBI:CHEBI:31832;
CC Evidence={ECO:0000269|PubMed:15668381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33612;
CC Evidence={ECO:0000269|PubMed:15668381};
CC -!- ACTIVITY REGULATION: Esterase activity is down-regulated by salicylic
CC acid (SA) or by tetraFA, a synthetic SA analog.
CC {ECO:0000269|PubMed:15668381, ECO:0000269|PubMed:19131332}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.6 uM for methyl salicylate (MeSA) {ECO:0000269|PubMed:15668381};
CC Note=kcat is 0.45 sec(-1) with methyl salicylate as substrate.
CC {ECO:0000269|PubMed:15668381};
CC -!- PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:15668381}.
CC -!- MISCELLANEOUS: Two amino acid substitutions near the catalytic pocket
CC are sufficient to switch from an esterase to a hydroxynitrile lyase
CC activity.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; AY485932; AAR87711.1; -; mRNA.
DR RefSeq; NP_001312442.1; NM_001325513.1.
DR PDB; 1XKL; X-ray; 2.00 A; A/B/C/D=1-260.
DR PDB; 1Y7H; X-ray; 2.52 A; A/B/C/D/E/F/G/H=1-260.
DR PDB; 1Y7I; X-ray; 2.10 A; A/B=1-260.
DR PDBsum; 1XKL; -.
DR PDBsum; 1Y7H; -.
DR PDBsum; 1Y7I; -.
DR AlphaFoldDB; Q6RYA0; -.
DR SMR; Q6RYA0; -.
DR STRING; 4097.A0A1S3ZW27; -.
DR DrugCentral; Q6RYA0; -.
DR ESTHER; nicta-SABP2; Hydroxynitrile_lyase.
DR GeneID; 107791137; -.
DR KEGG; nta:107791137; -.
DR OMA; SMAHEAW; -.
DR OrthoDB; 923240at2759; -.
DR BioCyc; MetaCyc:MON18C3-53; -.
DR SABIO-RK; Q6RYA0; -.
DR EvolutionaryTrace; Q6RYA0; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016298; F:lipase activity; IDA:UniProtKB.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IBA:GO_Central.
DR GO; GO:0080032; F:methyl jasmonate esterase activity; IBA:GO_Central.
DR GO; GO:0080031; F:methyl salicylate esterase activity; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009696; P:salicylic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR045889; MES/HNL.
DR PANTHER; PTHR10992; PTHR10992; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Immunity; Innate immunity; Plant defense;
KW Reference proteome.
FT CHAIN 1..260
FT /note="Salicylic acid-binding protein 2"
FT /id="PRO_0000418175"
FT ACT_SITE 81
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0000269|PubMed:17916738"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:15668381"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:17916738"
FT BINDING 13
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0007744|PDB:1Y7I"
FT BINDING 81
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0007744|PDB:1Y7I"
FT BINDING 159
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0007744|PDB:1Y7I"
FT BINDING 238
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0007744|PDB:1Y7I"
FT BINDING 253
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0007744|PDB:1Y7I"
FT BINDING 257
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0007744|PDB:1Y7I"
FT MUTAGEN 12
FT /note="G->T: Abolishes methyl salicylate esterase activity
FT and favors hydroxynitrile lyase activity; in association
FT with K-239."
FT /evidence="ECO:0000269|PubMed:20797615"
FT MUTAGEN 13
FT /note="A->L: Abolishes salicylic acid-binding."
FT /evidence="ECO:0000269|PubMed:17916738"
FT MUTAGEN 81
FT /note="S->A: Abolishes methyl salicylate esterase
FT activity."
FT /evidence="ECO:0000269|PubMed:15668381,
FT ECO:0000269|PubMed:17916738"
FT MUTAGEN 238
FT /note="H->A: Abolishes salicylic acid-binding and methyl
FT salicylate esterase activity."
FT /evidence="ECO:0000269|PubMed:17916738"
FT MUTAGEN 239
FT /note="M->K: Abolishes methyl salicylate esterase activity
FT and favors hydroxynitrile lyase activity; in association
FT with T-12."
FT /evidence="ECO:0000269|PubMed:20797615"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1XKL"
FT TURN 128..133
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1Y7I"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:1XKL"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1XKL"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:1XKL"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1XKL"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:1XKL"
SQ SEQUENCE 260 AA; 29304 MW; 9AA49E6423361145 CRC64;
MKEGKHFVLV HGACHGGWSW YKLKPLLEAA GHKVTALDLA ASGTDLRKIE ELRTLYDYTL
PLMELMESLS ADEKVILVGH SLGGMNLGLA MEKYPQKIYA AVFLAAFMPD SVHNSSFVLE
QYNERTPAEN WLDTQFLPYG SPEEPLTSMF FGPKFLAHKL YQLCSPEDLA LASSLVRPSS
LFMEDLSKAK YFTDERFGSV KRVYIVCTED KGIPEEFQRW QIDNIGVTEA IEIKGADHMA
MLCEPQKLCA SLLEIAHKYN
