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Protein

Thioesterase 1/protease 1/lysophospholipase L1

Gene

tesA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease (PubMed:8098033, PubMed:8432696, PubMed:1864840, PubMed:4945109, PubMed:4554913, PubMed:238979, PubMed:791643, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA (PubMed:8098033, PubMed:4554913, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate (PubMed:9070299). Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin and tributyrin, and p-nitrophenyl esters such as p-nitrophenyl hexanoate and p-nitrophenyl butyrate (PubMed:9070299). The protease activity is mainly active on small peptides (PubMed:8432696, PubMed:9070299). TesA is also able to hydrolyze p-nitrophenyl esters of N-substituted amino acids such as N-benzyloxycarbonyl-L-Phe-p-nitrophenyl ester (Z-L-Phe-ONp) and N-benzyloxycarbonyl-L-Tyr-p-nitrophenyl ester (Z-L-Tyr-ONp), however it is unable to hydrolyze N-acetyl-L-Phe ethyl ester and its Tyr analog (PubMed:8432696, PubMed:791643, PubMed:10423542). TesA also hydrolyzes N-benzyloxycarbonyl-L-Phe beta-nitrophenyl ester (Cbz-Phe-ONap) and N-acetyl-DL-Phe-2-naphthyl ester (chymotrypsin-like specificity) (PubMed:8432696, PubMed:4945109). Shows a slow proteolytic activity against denatured casein (PubMed:4945109). The lysophospholipase activity of TesA is able to hydrolyze 1-palmitoyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoglycerol, 1- and 2-acyl-sn-glycero-3-phosphoethanolamine (PubMed:1864840, PubMed:238979, PubMed:10423542).10 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Thioesterase activity is inhibited by iodoacetamide and photoactivated methylene blue, and slowly inhibited by 2,4-dinitrofluorobenzene (PubMed:4554913). Protease and lysophospholipase activities are inhibited by diisopropylfluorophosphate (DFP) (PubMed:1864840, PubMed:4945109, PubMed:238979). Lysophospholipase activity is inhibited by Fe2+, Fe3+ and Al3+ ions (PubMed:238979). Diethyl p-nitrophenyl phosphate (DENP) irreversibly inhibits both the protease and thioesterase activities (PubMed:12846577).5 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). Kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). Kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:16515533). Kcat is 14.1 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:9070299). Kcat is 10.13 sec(-1) for lauroyl-CoA as substrate (PubMed:16515533). Kcat is 5.1 sec(-1) for p-nitrophenyl decaonate as substrate (PubMed:9070299). Kcat is 2.6 sec(-1) for palmitoyl-CoA as substrate (PubMed:9070299). Kcat is 2.3 sec(-1) for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl ester as substrate (PubMed:9070299).2 Publications
  1. KM=3.5 µM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester1 Publication
  2. KM=3.8 µM for oleyl-ACP1 Publication
  3. KM=4 µM for oleyl-CoA1 Publication
  4. KM=4 µM for palmitoleoyl-CoA1 Publication
  5. KM=4.6 µM for cis-vaccenoyl-CoA1 Publication
  6. KM=6.2 µM for palmitoyl-CoA1 Publication
  7. KM=6.4 µM for myristoyl-CoA1 Publication
  8. KM=7.2 µM for palmitoyl-CoA1 Publication
  9. KM=7.7 µM for stearoyl-CoA1 Publication
  10. KM=9.9 µM for arachidoyl-CoA1 Publication
  11. KM=11.5 µM for decanoyl-CoA1 Publication
  12. KM=13.2 µM for N-benzyloxycarbonyl-D-tyrosine-p-nitrophenyl ester1 Publication
  13. KM=27.3 µM for hexanoyl-CoA1 Publication
  14. KM=110 µM for oleyl pantetheine1 Publication
  15. KM=146 µM for lauroyl-CoA (at pH 7 and 37 degrees Celsius)1 Publication
  16. KM=174 µM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester (at pH 7 and 37 degrees Celsius)1 Publication
  17. KM=200 µM for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester1 Publication
  18. KM=730 µM for diethyl p-nitrophenyl phosphate1 Publication
  19. KM=617.8 µM for p-nitrophenyl decaonate1 Publication
  20. KM=870 µM for p-nitrophenyl butyrate (at pH 7 and 37 degrees Celsius)1 Publication
  21. KM=1.46 mM for p-nitrophenyl butyrate1 Publication
  1. Vmax=25 µmol/min/mg enzyme with N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate1 Publication
  2. Vmax=0.33 µmol/min/mg enzyme with diethyl p-nitrophenyl phosphate as substrate1 Publication
  3. Vmax=30.1 pmol/min/mg enzyme with palmitoyl-CoA as substrate1 Publication
  4. Vmax=20.9 pmol/min/mg enzyme with myristoyl-CoA as substrate1 Publication
  5. Vmax=19.7 pmol/min/mg enzyme with stearoyl-CoA as substrate1 Publication
  6. Vmax=19.3 pmol/min/mg enzyme with cis-vaccenoyl-CoA as substrate1 Publication
  7. Vmax=17 pmol/min/mg enzyme with arachidoyl-CoA as substrate1 Publication
  8. Vmax=15.7 pmol/min/mg enzyme with palmitoleoyl-CoA as substrate1 Publication
  9. Vmax=14 pmol/min/mg enzyme with oleyl-CoA as substrate1 Publication
  10. Vmax=9.6 pmol/min/mg enzyme with decanoyl-CoA as substrate1 Publication
  11. Vmax=7.7 pmol/min/mg enzyme with hexanoyl-CoA as substrate1 Publication
  12. Vmax=7.6 pmol/min/mg enzyme with oleyl pantetheine as substrate1 Publication
  13. Vmax=0.4 pmol/min/mg enzyme with oleyl-ACP as substrate1 Publication

pH dependencei

Optimum pH is 7.5-8.4 (PubMed:4945109, PubMed:4554913, PubMed:12846577). Stable between pH 6.1 and 12, however, below pH 6.0, thioesterase rapidly loses activity (PubMed:4554913).3 Publications

Temperature dependencei

Protease is stable up to 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei36Nucleophile3 Publications2 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei70Substrate; via amide nitrogen1 Publication1
Binding sitei99Substrate1 Publication1
Active sitei1802 Publications2 Publications1
Active sitei1832 Publications2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:THIOESTERI-MONOMER
MetaCyc:THIOESTERI-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.5 2026
3.1.2.2 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0ADA1

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001818

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Thioesterase 1/protease 1/lysophospholipase L11 Publication
Short name:
TAP1 Publication
Alternative name(s):
Acyl-CoA thioesterase 11 Publication (EC:3.1.2.21 Publication)
Short name:
TESA1 Publication
Acyl-CoA thioesterase I1 Publication
Arylesterase1 Publication (EC:3.1.1.21 Publication)
Lysophospholipase L11 Publication (EC:3.1.1.52 Publications)
Oleoyl-[acyl-carrier-protein] hydrolase1 Publication (EC:3.1.2.141 Publication)
Phospholipid degradation C1 Publication
Short name:
Pldc1 Publication
Protease 11 Publication (EC:3.4.21.-1 Publication)
Protease I1 Publication
Thioesterase I/protease I1 Publication
Short name:
TEP-I1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tesA1 Publication
Synonyms:apeA1 Publication, pldC1 Publication
Ordered Locus Names:b0494, JW0483
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG11542 tesA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

  • Periplasm 2 Publications

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene do not show thioesterase activity and have a little protease activity against Cbz-Phe-ONap. No effect on the cell growth and fatty acid composition.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi36S → A: Loss of hydrolysis activity. 1 Publication1
Mutagenesisi70G → A: Retains weak hydrolysis activity. 1 Publication1
Mutagenesisi99N → A: Retains weak hydrolysis activity. 1 Publication1
Mutagenesisi135L → P: Abolishes switch loop movement. Lowers activity towards substrates with long acyl chains. 1 Publication1
Mutagenesisi180D → A: Retains weak hydrolysis activity. 1 Publication1
Mutagenesisi183H → A: Loss of hydrolysis activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02364 2-Amino-3-(Diethoxy-Phosphoryloxy)-Propionic Acid
DB04519 Caprylic acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 263 PublicationsAdd BLAST26
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001784827 – 208Thioesterase 1/protease 1/lysophospholipase L1Add BLAST182

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0ADA1

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0ADA1

PRoteomics IDEntifications database

More...
PRIDEi
P0ADA1

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0ADA1

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer or homotetramer.5 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259854, 5 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0451

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0ADA1

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0ADA1

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0ADA1

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the 'GDSL' lipolytic enzyme family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108UJV Bacteria
COG2755 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000261382

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0ADA1

KEGG Orthology (KO)

More...
KOi
K10804

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0ADA1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1110, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008265 Lipase_GDSL_AS
IPR013830 SGNH_hydro
IPR036514 SGNH_hydro_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13472 Lipase_GDSL_2, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01098 LIPASE_GDSL_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0ADA1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMNFNNVFRW HLPFLFLVLL TFRAAAADTL LILGDSLSAG YRMSASAAWP
60 70 80 90 100
ALLNDKWQSK TSVVNASISG DTSQQGLARL PALLKQHQPR WVLVELGGND
110 120 130 140 150
GLRGFQPQQT EQTLRQILQD VKAANAEPLL MQIRLPANYG RRYNEAFSAI
160 170 180 190 200
YPKLAKEFDV PLLPFFMEEV YLKPQWMQDD GIHPNRDAQP FIADWMAKQL

QPLVNHDS
Length:208
Mass (Da):23,622
Last modified:December 6, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCD03F23EA39541F1
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB40248 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

Protein sequence database of the Protein Information Resource

More...
PIRi
A49699
PX0045

NCBI Reference Sequences

More...
RefSeqi
NP_415027.1, NC_000913.3
WP_001297298.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73596; AAC73596; b0494
BAE76273; BAE76273; BAE76273

Database of genes from NCBI RefSeq genomes

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GeneIDi
945127

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0483
eco:b0494

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.515

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_001297298.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IVNX-ray1.90A27-208[»]
1J00X-ray2.00A27-208[»]
1JRLX-ray1.95A27-208[»]
1U8UX-ray2.08A27-208[»]
1V2GX-ray2.00A27-208[»]
5TICX-ray1.65A/B28-208[»]
5TIDX-ray1.20A28-208[»]
5TIEX-ray1.15A28-208[»]
5TIFX-ray0.97A28-208[»]
ProteinModelPortaliP0ADA1
SMRiP0ADA1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259854, 5 interactors
STRINGi316385.ECDH10B_0451

Chemistry databases

DrugBankiDB02364 2-Amino-3-(Diethoxy-Phosphoryloxy)-Propionic Acid
DB04519 Caprylic acid
SwissLipidsiSLP:000001818

2D gel databases

SWISS-2DPAGEiP0ADA1

Proteomic databases

EPDiP0ADA1
PaxDbiP0ADA1
PRIDEiP0ADA1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73596; AAC73596; b0494
BAE76273; BAE76273; BAE76273
GeneIDi945127
KEGGiecj:JW0483
eco:b0494
PATRICifig|511145.12.peg.515

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB1504
EcoGeneiEG11542 tesA

Phylogenomic databases

eggNOGiENOG4108UJV Bacteria
COG2755 LUCA
HOGENOMiHOG000261382
InParanoidiP0ADA1
KOiK10804
PhylomeDBiP0ADA1

Enzyme and pathway databases

BioCyciEcoCyc:THIOESTERI-MONOMER
MetaCyc:THIOESTERI-MONOMER
BRENDAi3.1.1.5 2026
3.1.2.2 2026
SABIO-RKiP0ADA1

Miscellaneous databases

EvolutionaryTraceiP0ADA1

Protein Ontology

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PROi
PR:P0ADA1

Family and domain databases

Gene3Di3.40.50.1110, 1 hit
InterProiView protein in InterPro
IPR008265 Lipase_GDSL_AS
IPR013830 SGNH_hydro
IPR036514 SGNH_hydro_sf
PfamiView protein in Pfam
PF13472 Lipase_GDSL_2, 1 hit
PROSITEiView protein in PROSITE
PS01098 LIPASE_GDSL_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTESA_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0ADA1
Secondary accession number(s): P29679
, P37331, P77125, Q2MBT3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: December 5, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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