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Protein

Salicylic acid-binding protein 2

Gene

SABP2

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required to convert methyl salicylate (MeSA) to salicylic acid (SA) as part of the signal transduction pathways that activate systemic acquired resistance in systemic tissue. MeSA is believed to be an inactive form that needs to be demethylated to exert a biological effect. Also able to catalyze the conversion of acibenzolar-S-methyl into acibenzolar to induce systemic acquired resistance.6 Publications

Enzyme regulationi

Esterase activity is down-regulated by salicylic acid (SA) or by tetraFA, a synthetic SA analog.2 Publications

Kineticsi

  1. KM=8.6 µM for methyl salicylate (MeSA)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei81Acyl-ester intermediate1
    Active sitei210Charge relay system1
    Active sitei238Charge relay system1

    GO - Molecular functioni

    • lipase activity Source: UniProtKB
    • methyl salicylate esterase activity Source: UniProtKB

    GO - Biological processi

    • metabolic process Source: UniProtKB
    • systemic acquired resistance, salicylic acid mediated signaling pathway Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Immunity, Innate immunity, Plant defense

    Protein family/group databases

    ESTHERinicta-SABP2. Hydroxynitrile_lyase.
    MEROPSiS33.A63.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Salicylic acid-binding protein 2 (EC:3.1.1.-)
    Short name:
    NtSABP2
    Alternative name(s):
    Methyl salicylate esterase
    Gene namesi
    Name:SABP2
    OrganismiNicotiana tabacum (Common tobacco)
    Taxonomic identifieri4097 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi12G → T: Abolishes methyl salicylate esterase activity and favors hydroxynitrile lyase activity; in association with K-239. 1
    Mutagenesisi13A → L: Abolishes salicylic acid-binding. 1 Publication1
    Mutagenesisi81S → A: Abolishes methyl salicylate esterase activity. 2 Publications1
    Mutagenesisi238H → A: Abolishes salicylic acid-binding and methyl salicylate esterase activity. 1 Publication1
    Mutagenesisi239M → K: Abolishes methyl salicylate esterase activity and favors hydroxynitrile lyase activity; in association with T-12. 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004181751 – 260Salicylic acid-binding protein 2Add BLAST260

    Structurei

    Secondary structure

    1260
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 10Combined sources5
    Helixi17 – 20Combined sources4
    Helixi23 – 29Combined sources7
    Beta strandi33 – 36Combined sources4
    Helixi49 – 51Combined sources3
    Helixi55 – 67Combined sources13
    Beta strandi71 – 73Combined sources3
    Beta strandi75 – 80Combined sources6
    Helixi83 – 93Combined sources11
    Helixi95 – 97Combined sources3
    Beta strandi98 – 105Combined sources8
    Beta strandi111 – 113Combined sources3
    Helixi117 – 124Combined sources8
    Turni128 – 133Combined sources6
    Beta strandi135 – 138Combined sources4
    Beta strandi142 – 144Combined sources3
    Beta strandi147 – 150Combined sources4
    Helixi153 – 159Combined sources7
    Helixi166 – 175Combined sources10
    Helixi183 – 188Combined sources6
    Turni194 – 196Combined sources3
    Helixi197 – 199Combined sources3
    Beta strandi202 – 207Combined sources6
    Turni211 – 214Combined sources4
    Helixi215 – 225Combined sources11
    Beta strandi228 – 233Combined sources6
    Helixi240 – 243Combined sources4
    Helixi245 – 258Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1XKLX-ray2.00A/B/C/D1-260[»]
    1Y7HX-ray2.52A/B/C/D/E/F/G/H1-260[»]
    1Y7IX-ray2.10A/B1-260[»]
    ProteinModelPortaliQ6RYA0.
    SMRiQ6RYA0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6RYA0.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6RYA0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKEGKHFVLV HGACHGGWSW YKLKPLLEAA GHKVTALDLA ASGTDLRKIE
    60 70 80 90 100
    ELRTLYDYTL PLMELMESLS ADEKVILVGH SLGGMNLGLA MEKYPQKIYA
    110 120 130 140 150
    AVFLAAFMPD SVHNSSFVLE QYNERTPAEN WLDTQFLPYG SPEEPLTSMF
    160 170 180 190 200
    FGPKFLAHKL YQLCSPEDLA LASSLVRPSS LFMEDLSKAK YFTDERFGSV
    210 220 230 240 250
    KRVYIVCTED KGIPEEFQRW QIDNIGVTEA IEIKGADHMA MLCEPQKLCA
    260
    SLLEIAHKYN
    Length:260
    Mass (Da):29,304
    Last modified:July 5, 2004 - v1
    Checksum:i9AA49E6423361145
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY485932 mRNA. Translation: AAR87711.1.
    RefSeqiNP_001312442.1. NM_001325513.1.
    UniGeneiNta.4007.

    Genome annotation databases

    GeneIDi107791137.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY485932 mRNA. Translation: AAR87711.1.
    RefSeqiNP_001312442.1. NM_001325513.1.
    UniGeneiNta.4007.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1XKLX-ray2.00A/B/C/D1-260[»]
    1Y7HX-ray2.52A/B/C/D/E/F/G/H1-260[»]
    1Y7IX-ray2.10A/B1-260[»]
    ProteinModelPortaliQ6RYA0.
    SMRiQ6RYA0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERinicta-SABP2. Hydroxynitrile_lyase.
    MEROPSiS33.A63.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi107791137.

    Miscellaneous databases

    EvolutionaryTraceiQ6RYA0.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00120. LIPASE_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSABP2_TOBAC
    AccessioniPrimary (citable) accession number: Q6RYA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: July 5, 2004
    Last modified: November 2, 2016
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two amino acid substitutions near the catalytic pocket are sufficient to switch from an esterase to a hydroxynitrile lyase activity.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.