XlyA

• Description: N-acetylmuramoyl-L-alanine amidase
  
  

Gene name	xlyA
Synonyms
Essential	no
Product	N-acetylmuramoyl-L-alanine amidase
Function	PBSX prophage-mediated lysis
Gene expression levels in SubtiExpress: xlyA
MW, pI	31 kDa, 5.342
Gene length, protein length	891 bp, 297 aa
Immediate neighbours	xhlB, spoIISB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall degradation/ turnover, PBSX prophage

The gene

Basic information

• Locus tag: BSU12810

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides (according to Swiss-Prot)

• Protein family: LysM repeat (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • contains a N-acetylglucosamine-polymer-binding LysM domain PubMed
  • contains an amidase_2 domain (like BlyA, CwlA, CwlH, XlyB)

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:
  • extracellular (no signal peptide) PubMed

Database entries

• Structure: 3HMA PubMed

• UniProt: P39800

• KEGG entry: [2]

• E.C. number: 3.5.1.28

Expression and regulation

• Operon:

• Expression browser: xlyA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Lieh Yoon Low, Chen Yang, Marta Perego, Andrei Osterman, Robert Liddington
Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins.
J Biol Chem: 2011, 286(39);34391-403
[PubMed:21816821] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

S Krogh, S T Jørgensen, K M Devine
Lysis genes of the Bacillus subtilis defective prophage PBSX.
J Bacteriol: 1998, 180(8);2110-7
[PubMed:9555893] [WorldCat.org] [DOI] (P p)

P F Longchamp, C Mauël, D Karamata
Lytic enzymes associated with defective prophages of Bacillus subtilis: sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX.
Microbiology (Reading): 1994, 140 ( Pt 8);1855-67
[PubMed:7921239] [WorldCat.org] [DOI] (P p)