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P37957

- ESTA_BACSU

UniProt

P37957 - ESTA_BACSU

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Protein
Lipase EstA
Gene
estA, lip, lipA, BSU02700
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 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.

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.

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 – 3131
Add
BLAST
Chaini32 – 212181Lipase EstA
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP37957.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1075.
HOGENOMiHOG000008725.
KOiK01046.
OMAiQIHGVGH.
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

MKFVKRRIIA LVTILMLSVT SLFALQPSAK AAEHNPVVMV HGIGGASFNF    50
AGIKSYLVSQ GWSRDKLYAV DFWDKTGTNY NNGPVLSRFV QKVLDETGAK 100
KVDIVAHSMG GANTLYYIKN LDGGNKVANV VTLGGANRLT TGKALPGTDP 150
NQKILYTSIY SSADMIVMNY LSRLDGARNV QIHGVGHIGL LYSSQVNSLI 200
KEGLNGGGQN TN 212
Length:212
Mass (Da):22,791
Last modified:May 30, 2000 - v2
Checksum:iB8A70E027461188F
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S23934.
RefSeqi NP_388152.1. NC_000964.3.
WP_003246250.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I6W X-ray 1.50 A/B 32-212 [» ]
1ISP X-ray 1.30 A 32-212 [» ]
1R4Z X-ray 1.80 A/B 32-212 [» ]
1R50 X-ray 1.45 A/B 32-212 [» ]
1T2N X-ray 1.80 A 32-212 [» ]
1T4M X-ray 2.00 A 32-212 [» ]
2QXT X-ray 2.00 A/B 34-212 [» ]
2QXU X-ray 1.90 A/B/C/D/E/F/G/H 34-212 [» ]
3D2A X-ray 1.73 A 32-212 [» ]
3D2B X-ray 1.95 A/B 32-212 [» ]
3D2C X-ray 2.18 A/B/C/D/E/F/G/H/I/J/K/L 32-212 [» ]
3QMM X-ray 1.89 A/B 32-212 [» ]
3QZU X-ray 1.85 A/B 32-212 [» ]
ProteinModelPortali P37957.
SMRi P37957. Positions 33-211.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU02700.

Proteomic databases

PaxDbi P37957.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12064 ; CAB12064 ; BSU02700 .
GeneIDi 938389.
KEGGi bsu:BSU02700.
PATRICi 18972099. VBIBacSub10457_0278.

Organism-specific databases

GenoListi BSU02700. [Micado ]

Phylogenomic databases

eggNOGi COG1075.
HOGENOMi HOG000008725.
KOi K01046.
OMAi QIHGVGH.
OrthoDBi EOG6W9X8D.
PhylomeDBi P37957.

Enzyme and pathway databases

BioCyci BSUB:BSU02700-MONOMER.

Miscellaneous databases

EvolutionaryTracei P37957.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view ]
Pfami PF01674. Lipase_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 109 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

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