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Conserved domains on  [gi|971749661|ref|YP_009203441|]
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endolysin [Mannheimia phage vB_MhS_535AP2]

Protein Classification

lysozyme( domain architecture ID 13014142)

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
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 30-183 9.29e-74

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: 218.24  E-value: 9.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  30 RTNQAGLEIIGNAEGCRRDPYKCPADVITVGIGSTEfggeKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNGKDMNDN 109
Cdd:cd16901    1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971749661 110 QFSGMTSAVFNMGCYNMRfyrnkqgqyvQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCL 183
Cdd:cd16901   77 EFDAYVSFAFNVGCGAFC----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 30-183 9.29e-74

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: 218.24  E-value: 9.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  30 RTNQAGLEIIGNAEGCRRDPYKCPADVITVGIGSTEfggeKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNGKDMNDN 109
Cdd:cd16901    1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971749661 110 QFSGMTSAVFNMGCYNMRfyrnkqgqyvQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCL 183
Cdd:cd16901   77 EFDAYVSFAFNVGCGAFC----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
30-186 7.99e-48

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 152.69  E-value: 7.99e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  30 RTNQAGLEIIGNAEGCRRDPYKCPADVITVGIGSTefgGEKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFnGKDMNDN 109
Cdd:COG3772    3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQN 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971749661 110 QFSGMTSAVFNMGCYNMRfyrnkqgqyvQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCLTGL 186
Cdd:COG3772   79 QFDALVSFAYNVGAGAFC----------RSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 58-176 3.51e-27

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 98.97  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661   58 TVGIGSTefgGEKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNGKDMNDNQFSGMTSAVFNMGCYNMRFyrnkqgqyv 137
Cdd:pfam00959   3 TIGIGHN---GKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGF--------- 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 971749661  138 qTTIHKLAVNKQFEEMCHRLPDFIRAsGKVLNGLVIRRE 176
Cdd:pfam00959  71 -STLLRAGNIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 30-183 9.29e-74

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: 218.24  E-value: 9.29e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  30 RTNQAGLEIIGNAEGCRRDPYKCPADVITVGIGSTEfggeKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNGKDMNDN 109
Cdd:cd16901    1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTH----GVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971749661 110 QFSGMTSAVFNMGCYNMRfyrnkqgqyvQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCL 183
Cdd:cd16901   77 EFDAYVSFAFNVGCGAFC----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
30-186 7.99e-48

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 152.69  E-value: 7.99e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  30 RTNQAGLEIIGNAEGCRRDPYKCPADVITVGIGSTefgGEKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFnGKDMNDN 109
Cdd:COG3772    3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHT---GKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQN 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 971749661 110 QFSGMTSAVFNMGCYNMRfyrnkqgqyvQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCLTGL 186
Cdd:COG3772   79 QFDALVSFAYNVGAGAFC----------RSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 35-183 2.93e-34

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: 118.00  E-value: 2.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  35 GLEIIGNAEGCRRDPYKCPADVITVGIGSTefGGEKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNgKDMNDNQFSGM 114
Cdd:cd00737    1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHT--GGVVVKPGDTITEAQAEALLRQDLARFEAAVNRLVK-VPLNQNQFDAL 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 971749661 115 TSAVFNMGCYNMRfyrnkqgqyvQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCL 183
Cdd:cd00737   78 VSFAFNVGAGAFK----------SSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 58-176 3.51e-27

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 98.97  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661   58 TVGIGSTefgGEKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNGKDMNDNQFSGMTSAVFNMGCYNMRFyrnkqgqyv 137
Cdd:pfam00959   3 TIGIGHN---GKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGCGKRGF--------- 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 971749661  138 qTTIHKLAVNKQFEEMCHRLPDFIRAsGKVLNGLVIRRE 176
Cdd:pfam00959  71 -STLLRAGNIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 38-183 1.84e-19

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: 79.91  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  38 IIGNAEGCRRDPYKCPADVITVGIGSTefgGEKIDPNRIYSDKEIAERWAKDLKIAESCVNRHFNGkDMNDNQFSGMTSA 117
Cdd:cd16900   11 LVGPWEGLRLTAYRDPVGVWTVCYGHT---GGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKV-PLPDPQRAALASF 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 971749661 118 VFNMGcynmrfyrnkQGQYVQTTIHKLAVNKQFEEMCHRLPDFIRASGKVLNGLVIRREKEKALCL 183
Cdd:cd16900   87 AYNVG----------VGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
chitinase-like cd16889
chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, ...
 35-120 1.41e-03

chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, and endolysin, which are involved in the degradation of 1,4-N-acetyl D-glucosamine linkages in chitin polymers and related activities. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitosanase enzymes hydrolyze chitosan, a biopolymer of beta (1,4)-linked-D-glucosamine (GlcN) residues produced by partial or full deacetylation of chitin. Pesticin (Pst) is a anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. 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.


Pssm-ID: 381610  Cd Length: 105  Bit Score: 36.78  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971749661  35 GLEIIGNAEGCRRDPYK-----CPADVITVGIGSTEFGGEKIDPNRIY------------SDKEIAERWAKDLKIAESCV 97
Cdd:cd16889    1 WFLLITSLETKGLGPTAvygdgKDPRGYTRGIGVTHGMLRGSTSRFPGvdtsnqtnngasTDSQLAKLAMEGFDPAYRAL 80

                         90       100
                 ....*....|....*....|....*
gi 971749661  98 NRHFNG--KDMNDNQFSGMTSAVFN 120
Cdd:cd16889   81 MRTIAHrdDLSPHVNGCAVIFAGFN 105
 
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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