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UniProtKB - P37957 (ESTA_BACSU)

Entry version 143 (07 Apr 2021)
Sequence version 2 (30 May 2000)
Previous versions | rss
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Protein

Lipase EstA

Gene

estA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score:

Annotation score:4 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

Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Strongly inhibited when incubated with the serine reagent phenylmethylsulfonyl fluoride. Activated by the addition of calcium to the reaction mixture. When calcium was incubated with the lipase but not added to the reaction mixture, its effect is lower but still observable. Magnesium, manganese and strontium are not able to replace calcium with full retention of activity.1 Publication

<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>pH dependencei

Optimum pH is 10. The activity decreases strongly above pH 10.5 or below pH 6.5. The enzyme is remarkably stable at alkaline pH, showing maximum stability at pH 12 and retaining more than 65% of its activity after 24 hours at pH 13.1 Publication

Temperature dependencei

Optimum temperature is 35 degrees Celsius. Stable for at least 30 minutes at 40 degrees Celsius. Virtually no activity remains after 30 minutes at 55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei108Nucleophile1
Active sitei164Charge relay system1
Active sitei187Charge relay system1

<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

  • lipase activity Source: GO_Central
  • triglyceride lipase activity Source: CACAO
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		BSUB:BSU02700-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P37957

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		bacsu-lip, Lipase_2

<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%5Fand%5Ftaxonomy%5Fsection">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:
Lipase EstA
Alternative name(s):
Lipase A (EC:3.1.1.3)
Triacylglycerol lipase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:estA
Synonyms:lip, lipA
Ordered Locus Names:BSU02700
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

Keywords - Cellular componenti

Secreted

<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

Chemistry databases

Drug and drug target database

More...DrugBanki		DB08475, [(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl hydrogen hex-5-enylphosphonate
DB08548, [(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl hydrogen hex-5-enylphosphonate

<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 – 31Add BLAST31
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001781932 – 212Lipase EstAAdd BLAST181

Proteomic databases

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

More...PaxDbi		P37957

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Maximally expressed in late exponential growth phase. Expression decreases rapidly in the stationary phase. Expressed in both rich and minimal media.2 Publications

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		224308.BSU02700

<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

1212
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P37957

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

More...SMRi		P37957

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P37957

<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 AB hydrolase superfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1075, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P37957

Identification of Orthologs from Complete Genome Data

More...OMAi		MIVMNYL

Database for complete collections of gene phylogenies

More...PhylomeDBi		P37957

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058, AB_hydrolase
IPR002918, Lipase_EstA/Esterase_EstB

The PANTHER Classification System

More...PANTHERi		PTHR32015, PTHR32015, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01674, Lipase_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53474, SSF53474, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P37957-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKFVKRRIIA LVTILMLSVT SLFALQPSAK AAEHNPVVMV HGIGGASFNF 
        60         70         80         90        100
AGIKSYLVSQ GWSRDKLYAV DFWDKTGTNY NNGPVLSRFV QKVLDETGAK 
       110        120        130        140        150
KVDIVAHSMG GANTLYYIKN LDGGNKVANV VTLGGANRLT TGKALPGTDP 
       160        170        180        190        200
NQKILYTSIY SSADMIVMNY LSRLDGARNV QIHGVGHIGL LYSSQVNSLI 
       210 
KEGLNGGGQN TN
Length:212
Mass (Da):22,791
Last modified:May 30, 2000 - v2
<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:iB8A70E027461188F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti29A → V in ABB54395 (Ref. 3) Curated1
Sequence conflicti51A → G in ABB54395 (Ref. 3) Curated1
Sequence conflicti60Q → H in ABB54395 (Ref. 3) Curated1
Sequence conflicti133L → V (PubMed:1320940).Curated1
Sequence conflicti133L → V (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M74010 Genomic DNA Translation: AAA22574.1
AB000617 Genomic DNA Translation: BAA22231.1
DQ250714 Genomic DNA Translation: ABB54395.1
AL009126 Genomic DNA Translation: CAB12064.1

Protein sequence database of the Protein Information Resource

More...PIRi		S23934

NCBI Reference Sequences

More...RefSeqi		NP_388152.1, NC_000964.3
WP_003246250.1, NZ_JNCM01000030.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CAB12064; CAB12064; BSU_02700

Database of genes from NCBI RefSeq genomes

More...GeneIDi		938389

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bsu:BSU02700

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224308.179.peg.280

<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
M74010 Genomic DNA Translation: AAA22574.1
AB000617 Genomic DNA Translation: BAA22231.1
DQ250714 Genomic DNA Translation: ABB54395.1
AL009126 Genomic DNA Translation: CAB12064.1
PIRiS23934
RefSeqiNP_388152.1, NC_000964.3
WP_003246250.1, NZ_JNCM01000030.1

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
1I6WX-ray1.50A/B32-212[»]
1ISPX-ray1.30A32-212[»]
1R4ZX-ray1.80A/B32-212[»]
1R50X-ray1.45A/B32-212[»]
1T2NX-ray1.80A32-212[»]
1T4MX-ray2.00A32-212[»]
2QXTX-ray2.00A/B34-212[»]
2QXUX-ray1.90A/B/C/D/E/F/G/H34-212[»]
3D2AX-ray1.73A32-212[»]
3D2BX-ray1.95A/B32-212[»]
3D2CX-ray2.18A/B/C/D/E/F/G/H/I/J/K/L32-212[»]
3QMMX-ray1.89A/B32-212[»]
3QZUX-ray1.85A/B32-212[»]
5CRIX-ray1.63A/B32-212[»]
5CT4X-ray1.49A/B33-212[»]
5CT5X-ray1.75A/B33-212[»]
5CT6X-ray1.90A/B33-212[»]
5CT8X-ray1.29A33-212[»]
5CT9X-ray1.40A33-212[»]
5CTAX-ray1.24A33-212[»]
5CURX-ray1.30A33-212[»]
BMRBiP37957
SMRiP37957
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU02700

Chemistry databases

DrugBankiDB08475, [(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl hydrogen hex-5-enylphosphonate
DB08548, [(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl hydrogen hex-5-enylphosphonate

Protein family/group databases

ESTHERibacsu-lip, Lipase_2

Proteomic databases

PaxDbiP37957

Genome annotation databases

EnsemblBacteriaiCAB12064; CAB12064; BSU_02700
GeneIDi938389
KEGGibsu:BSU02700
PATRICifig|224308.179.peg.280

Phylogenomic databases

eggNOGiCOG1075, Bacteria
InParanoidiP37957
OMAiMIVMNYL
PhylomeDBiP37957

Enzyme and pathway databases

BioCyciBSUB:BSU02700-MONOMER
SABIO-RKiP37957

Miscellaneous databases

EvolutionaryTraceiP37957

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR002918, Lipase_EstA/Esterase_EstB
PANTHERiPTHR32015, PTHR32015, 1 hit
PfamiView protein in Pfam
PF01674, Lipase_2, 1 hit
SUPFAMiSSF53474, SSF53474, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiESTA_BACSU
<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: P37957
Secondary accession number(s): O34644, Q2XU59
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: April 7, 2021
This is version 143 of the entry and version 2 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, Reference proteome

Documents

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