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Conserved domains on  [gi|90111309|ref|NP_416156|]
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inhibitor of c-type lysozyme, putative lipoprotein [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

C-type lysozyme inhibitor( domain architecture ID 10013787)

C-type lysozyme inhibitor specifically inhibits C-type lysozymes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11372 PRK11372
C-type lysozyme inhibitor;
1-109 4.25e-74

C-type lysozyme inhibitor;


:

Pssm-ID: 236902  Cd Length: 109  Bit Score: 214.71  E-value: 4.25e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309    1 MTMKKLLIIILPVLLSGCSAFNQLVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISASGARYTDGIY 80
Cdd:PRK11372   1 MSMKKLLIICLPVLLTGCSAYNQFVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISASGARYTDGIY 80

                         90       100
                 ....*....|....*....|....*....
gi 90111309   81 VFWSKGDEATVYKRDRIVLNNCQLQNPQR 109
Cdd:PRK11372  81 VFWSKGDEATVYKRDRIVLNNCQLQNPKR 109
 
Name Accession Description Interval E-value
PRK11372 PRK11372
C-type lysozyme inhibitor;
1-109 4.25e-74

C-type lysozyme inhibitor;


Pssm-ID: 236902  Cd Length: 109  Bit Score: 214.71  E-value: 4.25e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309    1 MTMKKLLIIILPVLLSGCSAFNQLVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISASGARYTDGIY 80
Cdd:PRK11372   1 MSMKKLLIICLPVLLTGCSAYNQFVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISASGARYTDGIY 80

                         90       100
                 ....*....|....*....|....*....
gi 90111309   81 VFWSKGDEATVYKRDRIVLNNCQLQNPQR 109
Cdd:PRK11372  81 VFWSKGDEATVYKRDRIVLNNCQLQNPKR 109
MliC COG3895
Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis];
3-106 1.35e-38

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


Pssm-ID: 443102  Cd Length: 108  Bit Score: 124.78  E-value: 1.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309   3 MKKLLIIILPVLLSGCSAFN-QLVERMQTDTLEYQCD-EKPLTVKLNNP-RQEVSFVYDNQLLHLKQGISASGARYTDGI 79
Cdd:COG3895   1 MKKLLLLLAALLLAGCASAApPADPAPATQTVHYQCEdGKPLTVTYINNdNSLAVLRLDGETLVLKQVVSASGARYSDGQ 80

                        90       100
                ....*....|....*....|....*...
gi 90111309  80 YVFWSKGDEATVYKR-DRIVLNNCQLQN 106
Cdd:COG3895  81 YVFWSKGDEATLERNgDDVVLNDCKLVK 108
MliC pfam09864
Membrane-bound lysozyme-inhibitor of c-type lysozyme; Lysozymes are ancient and important ...
 35-100 1.46e-20

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: 78.14  E-value: 1.46e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111309    35 YQCDEK-PLTVKLN-NPRQEVSFVYDNQLLHLKQGISASGARYTDGIYVFWSKGDEATVYKRDRIVLN 100
Cdd:pfam09864   1 YQCDDGeEVTVTYFdADPSTATLRLGGEQLVLPQVPSASGARYVGGGYEWWTKGNEATLTWGGKDPLQ 68
 
Name Accession Description Interval E-value
PRK11372 PRK11372
C-type lysozyme inhibitor;
1-109 4.25e-74

C-type lysozyme inhibitor;


Pssm-ID: 236902  Cd Length: 109  Bit Score: 214.71  E-value: 4.25e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309    1 MTMKKLLIIILPVLLSGCSAFNQLVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISASGARYTDGIY 80
Cdd:PRK11372   1 MSMKKLLIICLPVLLTGCSAYNQFVERMQTDTLEYQCDEKPLTVKLNNPRQEVSFVYDNQLLHLKQGISASGARYTDGIY 80

                         90       100
                 ....*....|....*....|....*....
gi 90111309   81 VFWSKGDEATVYKRDRIVLNNCQLQNPQR 109
Cdd:PRK11372  81 VFWSKGDEATVYKRDRIVLNNCQLQNPKR 109
MliC COG3895
Membrane-bound inhibitor of C-type lysozyme [Cell wall/membrane/envelope biogenesis];
3-106 1.35e-38

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


Pssm-ID: 443102  Cd Length: 108  Bit Score: 124.78  E-value: 1.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309   3 MKKLLIIILPVLLSGCSAFN-QLVERMQTDTLEYQCD-EKPLTVKLNNP-RQEVSFVYDNQLLHLKQGISASGARYTDGI 79
Cdd:COG3895   1 MKKLLLLLAALLLAGCASAApPADPAPATQTVHYQCEdGKPLTVTYINNdNSLAVLRLDGETLVLKQVVSASGARYSDGQ 80

                        90       100
                ....*....|....*....|....*...
gi 90111309  80 YVFWSKGDEATVYKR-DRIVLNNCQLQN 106
Cdd:COG3895  81 YVFWSKGDEATLERNgDDVVLNDCKLVK 108
MliC pfam09864
Membrane-bound lysozyme-inhibitor of c-type lysozyme; Lysozymes are ancient and important ...
 35-100 1.46e-20

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: 78.14  E-value: 1.46e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111309    35 YQCDEK-PLTVKLN-NPRQEVSFVYDNQLLHLKQGISASGARYTDGIYVFWSKGDEATVYKRDRIVLN 100
Cdd:pfam09864   1 YQCDDGeEVTVTYFdADPSTATLRLGGEQLVLPQVPSASGARYVGGGYEWWTKGNEATLTWGGKDPLQ 68
PRK13792 PRK13792
lysozyme inhibitor; Provisional
 27-92 1.43e-09

lysozyme inhibitor; Provisional


Pssm-ID: 106733  Cd Length: 127  Bit Score: 51.64  E-value: 1.43e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309   27 RMQTDTLEYQCDE-KPLTVK-LNNPRQEVSFV--YDNQLLHLKQGISASGARYTDGIYVFWSKGDEATVY 92
Cdd:PRK13792  41 KLDTRSVDYKCENgRKFTVQyLNKGDNSLAVVpvSDNSTLVFSNVISASGAKYAAGQYIWWTKGEEATLY 110
PRK13791 PRK13791
c-type lysozyme inhibitor;
35-105 6.17e-03

c-type lysozyme inhibitor;


Pssm-ID: 237508  Cd Length: 113  Bit Score: 33.70  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111309   35 YQC-DEKPLTVKLNNPRQEVSFVYDNQ---LLHLKQGISASGARYT----DGIYVFWSKGDEATVYKRD-RIVLNNCQLQ 105
Cdd:PRK13791  34 YTCnDNQVLEVIYVNTEAGNAYAIISQvdeMIPMRLMKMASGANYEainkNYTYKLYTKGKTAELVEGDdKPVLSNCSLA 113
 
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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