NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|486193269|ref|WP_001545200|]
View 

MULTISPECIES: lysozyme [Enterobacteriaceae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 11-172 3.69e-59

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: 180.83  E-value: 3.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  11 AAVLALIAAsapapdildQFLDEKEGNHTTAYRDGSGIWTICRGATmvdGKPVIPGMKLSKEKCAQVNAIERDKALAWVE 90
Cdd:cd16900    1 AGALALAAA---------ALVGPWEGLRLTAYRDPVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  91 RNIKVPLTEPQKAGIASFCpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRdcrirsnNCYGQVIRRDQESAL 170
Cdd:cd16900   69 RCVKVPLPDPQRAALASFA-YNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGR-------VLRGLVNRREAERAL 140


                 ..
gi 486193269 171 TC 172
Cdd:cd16900  141 CL 142
 
Name Accession Description Interval E-value
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 11-172 3.69e-59

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: 180.83  E-value: 3.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  11 AAVLALIAAsapapdildQFLDEKEGNHTTAYRDGSGIWTICRGATmvdGKPVIPGMKLSKEKCAQVNAIERDKALAWVE 90
Cdd:cd16900    1 AGALALAAA---------ALVGPWEGLRLTAYRDPVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  91 RNIKVPLTEPQKAGIASFCpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRdcrirsnNCYGQVIRRDQESAL 170
Cdd:cd16900   69 RCVKVPLPDPQRAALASFA-YNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGR-------VLRGLVNRREAERAL 140


                 ..
gi 486193269 171 TC 172
Cdd:cd16900  141 CL 142
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
23-175 1.70e-54

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 169.25  E-value: 1.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  23 APDILDQFLDEKEGNHTTAYRDGSGIWTICRGATmvdGKPVIPGMKLSKEKCAQVNAIERDKALAWVERNIKVPLTEPQK 102
Cdd:COG3772    4 TSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 486193269 103 AGIASFCpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRDCRirsnncyGQVIRRDQESALTCWGI 175
Cdd:COG3772   81 DALVSFA-YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLP-------GLVRRREAERALCLGGL 145
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 48-165 4.18e-33

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 113.60  E-value: 4.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269   48 IWTICRGatmVDGKPVIPGMKLSKEKCAQVNAIERDKALAWVERNIKVPLTEPQKAGIASFCPYNIGPGKCFPSTFYKRL 127
Cdd:pfam00959   1 YWTIGIG---HNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 486193269  128 NAGDRKGACEAIRWWIKDGgrdcrirsNNCYGQVIRRD 165
Cdd:pfam00959  78 NIGQWIKACSAIWKSLKAG--------KVYNGLVNRRE 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 ...
 11-172 3.69e-59

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: 180.83  E-value: 3.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  11 AAVLALIAAsapapdildQFLDEKEGNHTTAYRDGSGIWTICRGATmvdGKPVIPGMKLSKEKCAQVNAIERDKALAWVE 90
Cdd:cd16900    1 AGALALAAA---------ALVGPWEGLRLTAYRDPVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  91 RNIKVPLTEPQKAGIASFCpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRdcrirsnNCYGQVIRRDQESAL 170
Cdd:cd16900   69 RCVKVPLPDPQRAALASFA-YNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGR-------VLRGLVNRREAERAL 140


                 ..
gi 486193269 171 TC 172
Cdd:cd16900  141 CL 142
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
23-175 1.70e-54

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 169.25  E-value: 1.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  23 APDILDQFLDEKEGNHTTAYRDGSGIWTICRGATmvdGKPVIPGMKLSKEKCAQVNAIERDKALAWVERNIKVPLTEPQK 102
Cdd:COG3772    4 TSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 486193269 103 AGIASFCpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRDCRirsnncyGQVIRRDQESALTCWGI 175
Cdd:COG3772   81 DALVSFA-YNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLP-------GLVRRREAERALCLGGL 145
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 48-165 4.18e-33

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 113.60  E-value: 4.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269   48 IWTICRGatmVDGKPVIPGMKLSKEKCAQVNAIERDKALAWVERNIKVPLTEPQKAGIASFCPYNIGPGKCFPSTFYKRL 127
Cdd:pfam00959   1 YWTIGIG---HNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 486193269  128 NAGDRKGACEAIRWWIKDGgrdcrirsNNCYGQVIRRD 165
Cdd:pfam00959  78 NIGQWIKACSAIWKSLKAG--------KVYNGLVNRRE 107
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 29-170 6.83e-28

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: 101.06  E-value: 6.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  29 QFLDEKEGNHTTAYRDGSGIWTICRGATMVDGkpVIPGMKLSKEKCAQVNAIERDKALAWVERNIKVPLTEPQKAGIASF 108
Cdd:cd00737    3 DLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVV--VKPGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVSF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 486193269 109 CpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRDCRirsnncyGQVIRRDQESAL 170
Cdd:cd00737   81 A-FNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLP-------GLVRRRAAEAAL 134
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 8-170 1.49e-18

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: 77.26  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269   8 SLSAAVLALIAASapapdildqfldekEGNHTTAYRDGSGIWTICRGATMvdgkPVIPGMKLSKEKCAQvnAIERDKALA 87
Cdd:cd16901    1 RTSAAGLELIANA--------------EGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAK--RLAKDIKKA 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486193269  88 W--VERNI-KVPLTEPQKAGIASFCpYNIGPGKCFPSTFYKRLNAGDRKGACEAIRWWIKDGGRDcrirsnnCYGQVIRR 164
Cdd:cd16901   61 ErcVNRCFnGVPLPQGEFDAYVSFA-FNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKV-------LPGLVTRR 132


                 ....*.
gi 486193269 165 DQESAL 170
Cdd:cd16901  133 QKERAL 138
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH