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Conserved domains on  [gi|15595751|ref|NP_249245|]
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hypothetical protein PA0554 [Pseudomonas aeruginosa PAO1]

Protein Classification

MliC family protein( domain architecture ID 10561507)

MliC family protein similar to Cupriavidus necator membrane-bound lysozyme inhibitor of C-type lysozyme (MliC) that specifically inhibits C-type lysozymes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MliC pfam09864
Membrane-bound lysozyme-inhibitor of c-type lysozyme; Lysozymes are ancient and important ...
36-106 2.25e-15

Membrane-bound lysozyme-inhibitor of c-type lysozyme; 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. 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.


:

Pssm-ID: 462921  Cd Length: 68  Bit Score: 65.04  E-value: 2.25e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595751    36 WTCDSKAVIEWRYIDGSKNIVDLRLKDEddvVHHLEQEPAAVGAFYSDGRLGFHLENDEGLVYWVETDDLI 106
Cdd:pfam09864   1 YQCDDGEEVTVTYFDADPSTATLRLGGE---QLVLPQVPSASGARYVGGGYEWWTKGNEATLTWGGKDPLQ 68
 
Name Accession Description Interval E-value
MliC pfam09864
Membrane-bound lysozyme-inhibitor of c-type lysozyme; Lysozymes are ancient and important ...
36-106 2.25e-15

Membrane-bound lysozyme-inhibitor of c-type lysozyme; 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. 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.


Pssm-ID: 462921  Cd Length: 68  Bit Score: 65.04  E-value: 2.25e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595751    36 WTCDSKAVIEWRYIDGSKNIVDLRLKDEddvVHHLEQEPAAVGAFYSDGRLGFHLENDEGLVYWVETDDLI 106
Cdd:pfam09864   1 YQCDDGEEVTVTYFDADPSTATLRLGGE---QLVLPQVPSASGARYVGGGYEWWTKGNEATLTWGGKDPLQ 68
 
Name Accession Description Interval E-value
MliC pfam09864
Membrane-bound lysozyme-inhibitor of c-type lysozyme; Lysozymes are ancient and important ...
36-106 2.25e-15

Membrane-bound lysozyme-inhibitor of c-type lysozyme; 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. 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.


Pssm-ID: 462921  Cd Length: 68  Bit Score: 65.04  E-value: 2.25e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595751    36 WTCDSKAVIEWRYIDGSKNIVDLRLKDEddvVHHLEQEPAAVGAFYSDGRLGFHLENDEGLVYWVETDDLI 106
Cdd:pfam09864   1 YQCDDGEEVTVTYFDADPSTATLRLGGE---QLVLPQVPSASGARYVGGGYEWWTKGNEATLTWGGKDPLQ 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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