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Conserved domains on  [gi|992349889|ref|WP_061057433|]
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lysozyme [Morganella morganii]

Protein Classification

lysozyme( domain architecture ID 13014134)

lysozyme, also called endolysin or muramidase, hydrolyzes (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 15-154 1.26e-76

endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


:

Pssm-ID: 381619 [Multi-domain]  Cd Length: 142  Bit Score: 224.36  E-value: 1.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  15 GGAIAVALV-LIPAFEGMKFKPYQDVAGVWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRVDIPVYTR 93
Cdd:cd16900    1 AGALALAAAaLVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992349889  94 GAIYSFVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIEEVVC 154
Cdd:cd16900   81 AALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALC 141
 
Name Accession Description Interval E-value
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 15-154 1.26e-76

endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381619 [Multi-domain]  Cd Length: 142  Bit Score: 224.36  E-value: 1.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  15 GGAIAVALV-LIPAFEGMKFKPYQDVAGVWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRVDIPVYTR 93
Cdd:cd16900    1 AGALALAAAaLVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992349889  94 GAIYSFVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIEEVVC 154
Cdd:cd16900   81 AALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALC 141
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
15-156 1.50e-65

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 196.60  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  15 GGAIAVALVLIPAFEGMKFKPYQDVAGVWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRVDIPVYTRG 94
Cdd:COG3772    2 MKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992349889  95 AIYSFVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIEEVVCHG 156
Cdd:COG3772   82 ALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLG 143
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 42-148 6.73e-27

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 97.04  E-value: 6.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889   42 VWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRV-DIPVYTRGAIYSFVYNTGVGAFSRSTLLRKLNAG 120
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVkDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 992349889  121 DRVGACGEMKRWVFAgGKPWKGLMTRRE 148
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 107
 
Name Accession Description Interval E-value
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 15-154 1.26e-76

endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381619 [Multi-domain]  Cd Length: 142  Bit Score: 224.36  E-value: 1.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  15 GGAIAVALV-LIPAFEGMKFKPYQDVAGVWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRVDIPVYTR 93
Cdd:cd16900    1 AGALALAAAaLVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992349889  94 GAIYSFVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIEEVVC 154
Cdd:cd16900   81 AALASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALC 141
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
15-156 1.50e-65

Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 196.60  E-value: 1.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  15 GGAIAVALVLIPAFEGMKFKPYQDVAGVWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRVDIPVYTRG 94
Cdd:COG3772    2 MKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992349889  95 AIYSFVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIEEVVCHG 156
Cdd:COG3772   82 ALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLG 143
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 21-150 3.11e-54

endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381599 [Multi-domain]  Cd Length: 136  Bit Score: 167.31  E-value: 3.11e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  21 ALVLIPAFEGMKFKPYQDVAGVWTVCYGHTGSDIQR--DKIyTEAECKALLEKDLAVVAKGVDRLIRVDIPVYTRGAIYS 98
Cdd:cd00737    1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVVVKpgDTI-TEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 992349889  99 FVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIE 150
Cdd:cd00737   80 FAFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAE 131
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 19-154 6.87e-37

P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.


Pssm-ID: 381620 [Multi-domain]  Cd Length: 140  Bit Score: 123.49  E-value: 6.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  19 AVALVLIPAFEGMKFKPYQDVAGVWTVCYGHTGsDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIR-VDIPVYTRGAIY 97
Cdd:cd16901    4 AAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH-GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNgVPLPQGEFDAYV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 992349889  98 SFVYNTGVGAFSRSTLLRKLNAGDRVGACGEMKRWVFAGGKPWKGLMTRREIEEVVC 154
Cdd:cd16901   83 SFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALC 139
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 42-148 6.73e-27

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 97.04  E-value: 6.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889   42 VWTVCYGHTGSDIQRDKIYTEAECKALLEKDLAVVAKGVDRLIRV-DIPVYTRGAIYSFVYNTGVGAFSRSTLLRKLNAG 120
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVkDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 992349889  121 DRVGACGEMKRWVFAgGKPWKGLMTRRE 148
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 28-135 1.07e-10

bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.


Pssm-ID: 381597  Cd Length: 146  Bit Score: 56.23  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992349889  28 FEGMKFKPYQDVAGVWTVCYGHT-GSDIQRDKIY--TEAECKALLEKDLAVVAKGVDRLIRVDiPVY------TRGAIYS 98
Cdd:cd00735    9 DEGYRLKAYKDTEGYPTIGIGHLiGKKGASLTNGtiTKDEAEALFEQDVDRAVRDMLRNPKLA-PVYaqlnaaRRMALIN 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 992349889  99 FVYNTGVGAFSR-STLLRKLNAGDRVGACGEMKRWVFA 135
Cdd:cd00735   88 MAFQMGVGGLAKfKNMLAAIKAGDWEEAADGMLNSLWA 125
 
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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