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Protein

Lipase EstA

Gene

estA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme 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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Nucleophile
Active sitei164 – 1641Charge relay system
Active sitei187 – 1871Charge relay system

GO - Molecular functioni

  1. triglyceride lipase activity Source: CACAO

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU02700-MONOMER.
SABIO-RKP37957.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase EstA
Alternative name(s):
Lipase A (EC:3.1.1.3)
Triacylglycerol lipase
Gene namesi
Name:estA
Synonyms:lip, lipA
Ordered Locus Names:BSU02700
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU02700. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 212181Lipase EstAPRO_0000017819Add
BLAST

Proteomic databases

PaxDbiP37957.

Expressioni

Inductioni

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

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU02700.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 404Combined sources
Helixi47 – 504Combined sources
Helixi51 – 599Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 693Combined sources
Helixi79 – 9719Combined sources
Beta strandi102 – 1076Combined sources
Helixi110 – 12011Combined sources
Helixi123 – 1253Combined sources
Beta strandi127 – 1348Combined sources
Helixi137 – 1393Combined sources
Beta strandi155 – 1617Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 1724Combined sources
Beta strandi177 – 1848Combined sources
Helixi188 – 1925Combined sources
Helixi194 – 20411Combined sources
Turni205 – 2073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP37957.
SMRiP37957. Positions 33-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37957.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1075.
HOGENOMiHOG000008725.
InParanoidiP37957.
KOiK01046.
OMAiVMVHGIG.
OrthoDBiEOG6W9X8D.
PhylomeDBiP37957.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view]
PfamiPF01674. Lipase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

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
Checksum:iB8A70E027461188F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291A → V in ABB54395. 1 PublicationCurated
Sequence conflicti51 – 511A → G in ABB54395. 1 PublicationCurated
Sequence conflicti60 – 601Q → H in ABB54395. 1 PublicationCurated
Sequence conflicti133 – 1331L → V(PubMed:1320940)Curated
Sequence conflicti133 – 1331L → V1 PublicationCurated

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.

Genome annotation databases

EnsemblBacteriaiCAB12064; CAB12064; BSU02700.
GeneIDi938389.
KEGGibsu:BSU02700.
PATRICi18972099. VBIBacSub10457_0278.

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP37957.
SMRiP37957. Positions 33-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU02700.

Proteomic databases

PaxDbiP37957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12064; CAB12064; BSU02700.
GeneIDi938389.
KEGGibsu:BSU02700.
PATRICi18972099. VBIBacSub10457_0278.

Organism-specific databases

GenoListiBSU02700. [Micado]

Phylogenomic databases

eggNOGiCOG1075.
HOGENOMiHOG000008725.
InParanoidiP37957.
KOiK01046.
OMAiVMVHGIG.
OrthoDBiEOG6W9X8D.
PhylomeDBiP37957.

Enzyme and pathway databases

BioCyciBSUB:BSU02700-MONOMER.
SABIO-RKP37957.

Miscellaneous databases

EvolutionaryTraceiP37957.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view]
PfamiPF01674. Lipase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiESTA_BACSU
AccessioniPrimary (citable) accession number: P37957
Secondary accession number(s): O34644, Q2XU59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: January 7, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 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.