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P37957

- ESTA_BACSU

UniProt

P37957 - ESTA_BACSU

Protein

Lipase EstA

Gene

estA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37957.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily.Curated

    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

    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:
    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

    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: October 1, 2014
    This is version 110 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