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P37957 (ESTA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipase EstA
Alternative name(s):
Lipase A
EC=3.1.1.3
Triacylglycerol lipase
Gene names
Name:estA
Synonyms:lip, lipA
Ordered Locus Names:BSU02700
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups. Ref.5

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulation

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. Ref.5

Subcellular location

Secreted.

Induction

Maximally expressed in late exponential growth phase. Expression decreases rapidly in the stationary phase. Expressed in both rich and minimal media. Ref.5 Ref.6

Sequence similarities

Belongs to the AB hydrolase superfamily.

Biophysicochemical properties

pH dependence:

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. Ref.5

Temperature dependence:

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.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontriglyceride lipase activity

Inferred from direct assay Ref.5. Source: CACAO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 212181Lipase EstA
PRO_0000017819

Sites

Active site1081Nucleophile
Active site1641Charge relay system
Active site1871Charge relay system

Experimental info

Sequence conflict291A → V in ABB54395. Ref.3
Sequence conflict511A → G in ABB54395. Ref.3
Sequence conflict601Q → H in ABB54395. Ref.3
Sequence conflict1331L → V Ref.1
Sequence conflict1331L → V Ref.3

Secondary structure

.................................. 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37957 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: B8A70E027461188F

FASTA21222,791
        10         20         30         40         50         60 
MKFVKRRIIA LVTILMLSVT SLFALQPSAK AAEHNPVVMV HGIGGASFNF AGIKSYLVSQ 

        70         80         90        100        110        120 
GWSRDKLYAV DFWDKTGTNY NNGPVLSRFV QKVLDETGAK KVDIVAHSMG GANTLYYIKN 

       130        140        150        160        170        180 
LDGGNKVANV VTLGGANRLT TGKALPGTDP NQKILYTSIY SSADMIVMNY LSRLDGARNV 

       190        200        210 
QIHGVGHIGL LYSSQVNSLI KEGLNGGGQN TN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168."
Dartois V., Baulard A., Schanck K., Colson C.
Biochim. Biophys. Acta 1131:253-260(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"A 32 kb nucleotide sequence from the region of the lincomycin-resistance gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and identification of the site of the lin-2 mutation."
Kumano M., Tamakoshi A., Yamane K.
Microbiology 143:2775-2782(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"Molecular characterization of a lipase from a strain of Bacillus subtilis."
Peerzada K., Johri S., Rasool S., Andrabi K.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme."
Lesuisse E., Schanck K., Colson C.
Eur. J. Biochem. 216:155-160(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, N-TERMINAL END.
Strain: 168.
[6]"Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure."
Eggert T., van Pouderoyen G., Dijkstra B.W., Jaeger K.-E.
FEBS Lett. 502:89-92(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: 168 / BCL 1050.
[7]"The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme."
van Pouderoyen G., Eggert T., Jaeger K.-E., Dijkstra B.W.
J. Mol. Biol. 309:215-226(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-212.
[8]"Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution."
Kawasaki K., Kondo H., Suzuki M., Ohgiya S., Tsuda S.
Acta Crystallogr. D 58:1168-1174(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 32-212.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74010 Genomic DNA. Translation: AAA22574.1.
AB000617 Genomic DNA. Translation: BAA22231.1.
DQ250714 Genomic DNA. Translation: ABB54395.1.
AL009126 Genomic DNA. Translation: CAB12064.1.
PIRS23934.
RefSeqNP_388152.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP37957.
SMRP37957. Positions 33-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU02700.

Proteomic databases

PaxDbP37957.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12064; CAB12064; BSU02700.
GeneID938389.
KEGGbsu:BSU02700.
PATRIC18972099. VBIBacSub10457_0278.

Organism-specific databases

GenoListBSU02700. [Micado]

Phylogenomic databases

eggNOGCOG1075.
HOGENOMHOG000008725.
KOK01046.
OMAQIHGVGH.
OrthoDBEOG6W9X8D.
PhylomeDBP37957.

Enzyme and pathway databases

BioCycBSUB:BSU02700-MONOMER.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view]
PfamPF01674. Lipase_2. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37957.

Entry information

Entry nameESTA_BACSU
AccessionPrimary (citable) accession number: P37957
Secondary accession number(s): O34644, Q2XU59
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList