SMART: Pfam domain MliC

MliC

PFAM accession number:	PF09864
Interpro abstract (IPR018660):	Lysozymes are ancient and important components of the innate immune system of animals that hydrolyse peptidoglycan, the major bacterial cell wall polymer. Various mechanisms have evolved by which bacteria can evade this bactericidal enzyme, one being the production of lysozyme inhibitors. MliC (membrane bound lysozyme inhibitor of c-type lysozyme) of E. coli and Pseudomonas aeruginosa, possess lysozyme inhibitory activity and confer increased lysozyme tolerance upon expression in E. coli [ (PUBMED:18369469) ]. Structural analyses show that the invariant loop of MliC plays a crucial role in the inhibition of the lysozyme by its insertion into the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues [ (PUBMED:19028453) ]. Interestingly, lipoprotein LprI has a C-terminal MliC domain, and has been identified only in virulence-associated mycobacterial strains, where it acts as a lysozyme inhibitor [ (PUBMED:26589796) ].

PFAM accession number:

PF09864

Interpro abstract (IPR018660):

Lysozymes are ancient and important components of the innate immune system of animals that hydrolyse peptidoglycan, the major bacterial cell wall polymer. Various mechanisms have evolved by which bacteria can evade this bactericidal enzyme, one being the production of lysozyme inhibitors. MliC (membrane bound lysozyme inhibitor of c-type lysozyme) of E. coli and Pseudomonas aeruginosa, possess lysozyme inhibitory activity and confer increased lysozyme tolerance upon expression in E. coli [ (PUBMED:18369469) ]. Structural analyses show that the invariant loop of MliC plays a crucial role in the inhibition of the lysozyme by its insertion into the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues [ (PUBMED:19028453) ].

Interestingly, lipoprotein LprI has a C-terminal MliC domain, and has been identified only in virulence-associated mycobacterial strains, where it acts as a lysozyme inhibitor [ (PUBMED:26589796) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry MliC