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Conserved domains on  [gi|490822560|ref|WP_004684650|]
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MULTISPECIES: peptidoglycan hydrolase inhibitor PhiA [Brucella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MliC super family cl46353
Membrane-bound lysozyme-inhibitor of c-type lysozyme; Lysozymes are ancient and important ...
 57-158 4.03e-05

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.


The actual alignment was detected with superfamily member COG3895:

Pssm-ID: 480693  Cd Length: 108  Bit Score: 40.81  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822560  57 SAHAQADEEQPSIERVDYICERSVVVPVTYIrsNGAPAAAVLEVEGKMVALQwH---GDLKKYVAideqDSYRWADRGGQ 133
Cdd:COG3895   17 ASAAPPADPAPATQTVHYQCEDGKPLTVTYI--NNDNSLAVLRLDGETLVLK-QvvsASGARYSD----GQYVFWSKGDE 89

                         90       100
                 ....*....|....*....|....*
gi 490822560 134 ATLSHLEADhtakevTLLSACRADT 158
Cdd:COG3895   90 ATLERNGDD------VVLNDCKLVK 108
 
Name Accession Description Interval E-value
MliC COG3895
Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis];
57-158 4.03e-05

Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443102  Cd Length: 108  Bit Score: 40.81  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822560  57 SAHAQADEEQPSIERVDYICERSVVVPVTYIrsNGAPAAAVLEVEGKMVALQwH---GDLKKYVAideqDSYRWADRGGQ 133
Cdd:COG3895   17 ASAAPPADPAPATQTVHYQCEDGKPLTVTYI--NNDNSLAVLRLDGETLVLK-QvvsASGARYSD----GQYVFWSKGDE 89

                         90       100
                 ....*....|....*....|....*
gi 490822560 134 ATLSHLEADhtakevTLLSACRADT 158
Cdd:COG3895   90 ATLERNGDD------VVLNDCKLVK 108
 
Name Accession Description Interval E-value
MliC COG3895
Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis];
57-158 4.03e-05

Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443102  Cd Length: 108  Bit Score: 40.81  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490822560  57 SAHAQADEEQPSIERVDYICERSVVVPVTYIrsNGAPAAAVLEVEGKMVALQwH---GDLKKYVAideqDSYRWADRGGQ 133
Cdd:COG3895   17 ASAAPPADPAPATQTVHYQCEDGKPLTVTYI--NNDNSLAVLRLDGETLVLK-QvvsASGARYSD----GQYVFWSKGDE 89

                         90       100
                 ....*....|....*....|....*
gi 490822560 134 ATLSHLEADhtakevTLLSACRADT 158
Cdd:COG3895   90 ATLERNGDD------VVLNDCKLVK 108
 
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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