Lip

• Description: extracellular lipase
  
  

Gene name	lip
Synonyms	lipA
Essential	no
Product	extracellular lipase
Function	lipid degradation
MW, pI	22 kDa, 10.059
Gene length, protein length	636 bp, 212 aa
Immediate neighbours	ansZ, yczC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of lipids

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

• Locus tag: BSU02700

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): LipB

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2QXT

• UniProt: P37957

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: lip PubMed

• Sigma factor:

• Regulation:
  • repressed during vegetative growth (AbrB) PubMed

• Regulatory mechanism:
  • AbrB: transcription repression PubMed

• Additional information:
  • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

Bo Chen, Zhen Cai, Wei Wu, Yunlong Huang, Juergen Pleiss, Zhanglin Lin
Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.
Biochemistry: 2009, 48(48);11496-504
[PubMed:19883129] [WorldCat.org] [DOI] (I p)

Thijs R H M Kouwen, René van der Ploeg, Haike Antelmann, Michael Hecker, Georg Homuth, Ulrike Mäder, Jan Maarten van Dijl
Overflow of a hyper-produced secretory protein from the Bacillus Sec pathway into the Tat pathway for protein secretion as revealed by proteogenomics.
Proteomics: 2009, 9(4);1018-32
[PubMed:19180538] [WorldCat.org] [DOI] (I p)

Allison V Banse, Arnaud Chastanet, Lilah Rahn-Lee, Errett C Hobbs, Richard Losick
Parallel pathways of repression and antirepression governing the transition to stationary phase in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2008, 105(40);15547-52
[PubMed:18840696] [WorldCat.org] [DOI] (I p)

Ykelien L Boersma, Tjaard Pijning, Margriet S Bosma, Almer M van der Sloot, Luís F Godinho, Melloney J Dröge, Remko T Winter, Gertie van Pouderoyen, Bauke W Dijkstra, Wim J Quax
Loop grafting of Bacillus subtilis lipase A: inversion of enantioselectivity.
Chem Biol: 2008, 15(8);782-9
[PubMed:18721749] [WorldCat.org] [DOI] (P p)

Ykelien L Boersma, Melloney J Dröge, Almer M van der Sloot, Tjaard Pijning, Robbert H Cool, Bauke W Dijkstra, Wim J Quax
A novel genetic selection system for improved enantioselectivity of Bacillus subtilis lipase A.
Chembiochem: 2008, 9(7);1110-5
[PubMed:18383241] [WorldCat.org] [DOI] (I p)

Eerappa Rajakumara, Priyamvada Acharya, Shoeb Ahmad, Rajan Sankaranaryanan, Nalam M Rao
Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH.
Biochim Biophys Acta: 2008, 1784(2);302-11
[PubMed:18053819] [WorldCat.org] [DOI] (P p)

Melloney J Dröge, Ykelien L Boersma, Gertie van Pouderoyen, Titia E Vrenken, Carsten J Rüggeberg, Manfred T Reetz, Bauke W Dijkstra, Wim J Quax
Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection.
Chembiochem: 2006, 7(1);149-57
[PubMed:16342303] [WorldCat.org] [DOI] (P p)

Helga Westers, Peter G Braun, Lidia Westers, Haike Antelmann, Michael Hecker, Jan D H Jongbloed, Hirofumi Yoshikawa, Teruo Tanaka, Jan Maarten van Dijl, Wim J Quax
Genes involved in SkfA killing factor production protect a Bacillus subtilis lipase against proteolysis.
Appl Environ Microbiol: 2005, 71(4);1899-908
[PubMed:15812018] [WorldCat.org] [DOI] (P p)

Thorsten Eggert, Ulf Brockmeier, Melloney J Dröge, Wim J Quax, Karl-Erich Jaeger
Extracellular lipases from Bacillus subtilis: regulation of gene expression and enzyme activity by amino acid supply and external pH.
FEMS Microbiol Lett: 2003, 225(2);319-24
[PubMed:12951259] [WorldCat.org] [DOI] (P p)

Melloney J Dröge, Carsten J Rüggeberg, Almer M van der Sloot, Judith Schimmel, Dolf Swaving Dijkstra, Raymond M D Verhaert, Manfred T Reetz, Wim J Quax
Binding of phage displayed Bacillus subtilis lipase A to a phosphonate suicide inhibitor.
J Biotechnol: 2003, 101(1);19-28
[PubMed:12523966] [WorldCat.org] [DOI] (P p)

Jan D H Jongbloed, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Ulla Airaksinen, Frens Pries, Wim J Quax, Jan Maarten van Dijl, Peter G Braun
Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis.
J Biol Chem: 2002, 277(46);44068-78
[PubMed:12218047] [WorldCat.org] [DOI] (P p)

T Eggert, G van Pouderoyen, B W Dijkstra, K E Jaeger
Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure.
FEBS Lett: 2001, 502(3);89-92
[PubMed:11583117] [WorldCat.org] [DOI] (P p)

G van Pouderoyen, T Eggert, K E Jaeger, B W Dijkstra
The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme.
J Mol Biol: 2001, 309(1);215-26
[PubMed:11491291] [WorldCat.org] [DOI] (P p)

E Lesuisse, K Schanck, C Colson
Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme.
Eur J Biochem: 1993, 216(1);155-60
[PubMed:8396026] [WorldCat.org] [DOI] (P p)