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P0ADA1

- TESA_ECOLI

UniProt

P0ADA1 - TESA_ECOLI

Protein

Acyl-CoA thioesterase I

Gene

tesA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Hydrolyzes only long chain acyl thioesters (C12-C18). Specificity similar to chymotrypsin.

    Catalytic activityi

    2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361NucleophileBy similarity
    Binding sitei70 – 701Substrate; via amide nitrogen
    Binding sitei99 – 991Substrate
    Active sitei180 – 1801By similarity
    Active sitei183 – 18311 Publication

    GO - Molecular functioni

    1. acyl-CoA hydrolase activity Source: EcoCyc
    2. identical protein binding Source: EcoCyc
    3. lysophospholipase activity Source: EcoCyc
    4. palmitoyl-CoA hydrolase activity Source: EcoCyc
    5. peptidase activity Source: EcoCyc
    6. phospholipase activity Source: EcoCyc

    GO - Biological processi

    1. lipid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciEcoCyc:THIOESTERI-MONOMER.
    ECOL316407:JW0483-MONOMER.
    MetaCyc:THIOESTERI-MONOMER.
    SABIO-RKP0ADA1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA thioesterase I (EC:3.1.2.-)
    Alternative name(s):
    Lecithinase B
    Lysophospholipase L1 (EC:3.1.1.5)
    Protease I
    Gene namesi
    Name:tesA
    Synonyms:apeA, pldC
    Ordered Locus Names:b0494, JW0483
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11542. tesA.

    Subcellular locationi

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361S → A: Reduces activity by over 99%. 1 Publication
    Mutagenesisi70 – 701G → A: Reduces activity by over 75%. 1 Publication
    Mutagenesisi99 – 991N → A: Reduces activity by over 60%. 1 Publication
    Mutagenesisi135 – 1351L → P: Lowers activity towards substrates with long acyl chains.
    Mutagenesisi180 – 1801D → A: Reduces activity by over 70%. 1 Publication
    Mutagenesisi183 – 1831H → A: Reduces activity by over 99%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26262 PublicationsAdd
    BLAST
    Chaini27 – 208182Acyl-CoA thioesterase IPRO_0000017848Add
    BLAST

    Proteomic databases

    PaxDbiP0ADA1.
    PRIDEiP0ADA1.

    2D gel databases

    SWISS-2DPAGEP0ADA1.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ADA1.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi511145.b0494.

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 347
    Helixi36 – 394
    Beta strandi41 – 433
    Helixi45 – 473
    Helixi49 – 568
    Turni57 – 604
    Beta strandi61 – 655
    Helixi73 – 8715
    Beta strandi90 – 956
    Turni98 – 1014
    Beta strandi102 – 1043
    Helixi107 – 12317
    Beta strandi127 – 1315
    Helixi137 – 1393
    Helixi141 – 15717
    Helixi167 – 1715
    Helixi174 – 1763
    Beta strandi181 – 1844
    Helixi186 – 1883
    Helixi189 – 20012
    Turni201 – 2044

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IVNX-ray1.90A27-208[»]
    1J00X-ray2.00A27-208[»]
    1JRLX-ray1.95A27-208[»]
    1U8UX-ray2.08A27-208[»]
    1V2GX-ray2.00A27-208[»]
    ProteinModelPortaliP0ADA1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ADA1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 'GDSL' lipolytic enzyme family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2755.
    HOGENOMiHOG000261382.
    KOiK10804.
    OMAiRGFPPQQ.
    OrthoDBiEOG6PGK4B.
    PhylomeDBiP0ADA1.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR001087. Lipase_GDSL.
    IPR008265. Lipase_GDSL_AS.
    IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view]
    PfamiPF00657. Lipase_GDSL. 1 hit.
    [Graphical view]
    PROSITEiPS01098. LIPASE_GDSL_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0ADA1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP    50
    ALLNDKWQSK TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND 100
    GLRGFQPQQT EQTLRQILQD VKAANAEPLL MQIRLPANYG RRYNEAFSAI 150
    YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD GIHPNRDAQP FIADWMAKQL 200
    QPLVNHDS 208
    Length:208
    Mass (Da):23,622
    Last modified:December 6, 2005 - v1
    Checksum:iCD03F23EA39541F1
    GO

    Sequence cautioni

    The sequence AAB40248.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06182 Genomic DNA. Translation: AAA24664.1.
    D13180 Genomic DNA. Translation: BAA02475.1.
    U82664 Genomic DNA. Translation: AAB40248.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73596.1.
    AP009048 Genomic DNA. Translation: BAE76273.1.
    PIRiA49699.
    PX0045.
    RefSeqiNP_415027.1. NC_000913.3.
    YP_488785.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73596; AAC73596; b0494.
    BAE76273; BAE76273; BAE76273.
    GeneIDi12930860.
    945127.
    KEGGiecj:Y75_p0481.
    eco:b0494.
    PATRICi32116147. VBIEscCol129921_0515.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06182 Genomic DNA. Translation: AAA24664.1 .
    D13180 Genomic DNA. Translation: BAA02475.1 .
    U82664 Genomic DNA. Translation: AAB40248.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC73596.1 .
    AP009048 Genomic DNA. Translation: BAE76273.1 .
    PIRi A49699.
    PX0045.
    RefSeqi NP_415027.1. NC_000913.3.
    YP_488785.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IVN X-ray 1.90 A 27-208 [» ]
    1J00 X-ray 2.00 A 27-208 [» ]
    1JRL X-ray 1.95 A 27-208 [» ]
    1U8U X-ray 2.08 A 27-208 [» ]
    1V2G X-ray 2.00 A 27-208 [» ]
    ProteinModelPortali P0ADA1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 511145.b0494.

    2D gel databases

    SWISS-2DPAGE P0ADA1.

    Proteomic databases

    PaxDbi P0ADA1.
    PRIDEi P0ADA1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73596 ; AAC73596 ; b0494 .
    BAE76273 ; BAE76273 ; BAE76273 .
    GeneIDi 12930860.
    945127.
    KEGGi ecj:Y75_p0481.
    eco:b0494.
    PATRICi 32116147. VBIEscCol129921_0515.

    Organism-specific databases

    EchoBASEi EB1504.
    EcoGenei EG11542. tesA.

    Phylogenomic databases

    eggNOGi COG2755.
    HOGENOMi HOG000261382.
    KOi K10804.
    OMAi RGFPPQQ.
    OrthoDBi EOG6PGK4B.
    PhylomeDBi P0ADA1.

    Enzyme and pathway databases

    BioCyci EcoCyc:THIOESTERI-MONOMER.
    ECOL316407:JW0483-MONOMER.
    MetaCyc:THIOESTERI-MONOMER.
    SABIO-RK P0ADA1.

    Miscellaneous databases

    EvolutionaryTracei P0ADA1.
    PROi P0ADA1.

    Gene expression databases

    Genevestigatori P0ADA1.

    Family and domain databases

    Gene3Di 3.40.50.1110. 1 hit.
    InterProi IPR001087. Lipase_GDSL.
    IPR008265. Lipase_GDSL_AS.
    IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view ]
    Pfami PF00657. Lipase_GDSL. 1 hit.
    [Graphical view ]
    PROSITEi PS01098. LIPASE_GDSL_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme."
      Cho H., Cronan J.E. Jr.
      J. Biol. Chem. 268:9238-9245(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase-defective Escherichia coli mutants."
      Ichihara S., Matsubara Y., Kato C., Akasaka K., Mizushima S.
      J. Bacteriol. 175:1032-1037(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-38.
      Strain: K12.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Lysophospholipase L1 from Escherichia coli K-12 overproducer."
      Karasawa K., Kudo I., Kobayashi T., Homma H., Chiba N., Mizushima H., Inoue K., Nojima S.
      J. Biochem. 109:288-293(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-43, CHARACTERIZATION AS LYSOPHOSPHOLIPASE.
      Strain: K12.
    7. "Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1."
      Lee L.-C., Lee Y.-L., Leu R.-J., Shaw J.-F.
      Biochem. J. 397:69-76(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-36; GLY-70; ASN-99; ASP-180 AND HIS-183.
    8. "Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network."
      Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C.
      J. Mol. Biol. 330:539-551(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 27-208 IN COMPLEX WITH SUBSTRATE ANALOG, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement."
      Lo Y.-C., Lin S.-C., Shaw J.-F., Liaw Y.-C.
      Biochemistry 44:1971-1979(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 27-208 OF WILD-TYPE AND MUTANT PRO-135 IN COMPLEX WITH SUBSTRATE ANALOG.

    Entry informationi

    Entry nameiTESA_ECOLI
    AccessioniPrimary (citable) accession number: P0ADA1
    Secondary accession number(s): P29679
    , P37331, P77125, Q2MBT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3