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Conserved domains on  [gi|446599610|ref|WP_000676956|]
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MULTISPECIES: lysozyme [Enterobacteriaceae]

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 ...
 29-179 6.47e-78

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: 228.65  E-value: 6.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  29 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSA 108
Cdd:cd16901    1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446599610 109 MTSAAFNMGCNSLRtyyskargmrvETSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 179
Cdd:cd16901   81 YVSFAFNVGCGAFC-----------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 ...
 29-179 6.47e-78

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: 228.65  E-value: 6.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  29 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSA 108
Cdd:cd16901    1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446599610 109 MTSAAFNMGCNSLRtyyskargmrvETSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 179
Cdd:cd16901   81 YVSFAFNVGCGAFC-----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
29-182 4.43e-47

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 150.76  E-value: 4.43e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  29 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNT-HGVTPGVRKTDQQIAADWEKNILIAERCINQHFrGKDMPDNAFS 107
Cdd:COG3772    3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQNQFD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446599610 108 AMTSAAFNMGCNSLRTyyskargmrveTSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCLTGL 182
Cdd:COG3772   82 ALVSFAYNVGAGAFCR-----------STLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 55-172 1.97e-35

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 119.77  E-value: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610   55 VWTDGIG-NTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSAMTSAAFNMGCnslrtyyskarGMRV 133
Cdd:pfam00959   1 YWTIGIGhNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGC-----------GKRG 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446599610  134 ETSIHKWAQKGEWVNMCNHLPDFVNSnGVPLRGLKIRRE 172
Cdd:pfam00959  70 FSTLLRAGNIGQWIKACSAIWKSLKA-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 ...
 29-179 6.47e-78

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: 228.65  E-value: 6.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  29 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSA 108
Cdd:cd16901    1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446599610 109 MTSAAFNMGCNSLRtyyskargmrvETSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 179
Cdd:cd16901   81 YVSFAFNVGCGAFC-----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
29-182 4.43e-47

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 150.76  E-value: 4.43e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  29 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNT-HGVTPGVRKTDQQIAADWEKNILIAERCINQHFrGKDMPDNAFS 107
Cdd:COG3772    3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQNQFD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446599610 108 AMTSAAFNMGCNSLRTyyskargmrveTSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCLTGL 182
Cdd:COG3772   82 ALVSFAYNVGAGAFCR-----------STLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 34-179 3.61e-37

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: 125.32  E-value: 3.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  34 GLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGV--TPGVRKTDQQIAADWEKNILIAERCINQHFRgKDMPDNAFSAMTS 111
Cdd:cd00737    1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVvvKPGDTITEAQAEALLRQDLARFEAAVNRLVK-VPLNQNQFDALVS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446599610 112 AAFNMGCNSLRTyyskargmrveTSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 179
Cdd:cd00737   80 FAFNVGAGAFKS-----------STLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 55-172 1.97e-35

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 119.77  E-value: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610   55 VWTDGIG-NTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSAMTSAAFNMGCnslrtyyskarGMRV 133
Cdd:pfam00959   1 YWTIGIGhNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGC-----------GKRG 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446599610  134 ETSIHKWAQKGEWVNMCNHLPDFVNSnGVPLRGLKIRRE 172
Cdd:pfam00959  70 FSTLLRAGNIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
chitinase-like cd16889
chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, ...
 34-115 1.22e-16

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: 71.45  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  34 GLELIGNAEGCRRDPY-----MCPAGVWTDGIGNTHGVTPG----------------VRKTDQQIAADWEKNILIAERCI 92
Cdd:cd16889    1 WFLLITSLETKGLGPTavygdGKDPRGYTRGIGVTHGMLRGstsrfpgvdtsnqtnnGASTDSQLAKLAMEGFDPAYRAL 80

                         90       100
                 ....*....|....*....|....*
gi 446599610  93 NQHF--RGKDMPDNAFSAMTSAAFN 115
Cdd:cd16889   81 MRTIahRDDLSPHVNGCAVIFAGFN 105
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 37-179 5.49e-16

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: 70.66  E-value: 5.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610  37 LIGNAEGCRRDPYMCPAGVWT--DGIgnTHG-VTPGVRKTDQQIAADWEKNILIAERCINQHFRGkDMPDNAFSAMTSAA 113
Cdd:cd16900   11 LVGPWEGLRLTAYRDPVGVWTvcYGH--TGGdVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKV-PLPDPQRAALASFA 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599610 114 FNMG----CNSlrtyyskargmrvetSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 179
Cdd:cd16900   88 YNVGvgafCRS---------------TLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 34-87 2.02e-03

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 35.08  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446599610  34 GLELIGNAEGCRRDPYMCPAGVWTDGIG-NTHGVTPGVRK----TDQQIAADWEKNILI 87
Cdd:cd00442    1 VLAAIIGQESGGNKPANAGSGSGAAGLFqFMPGTWKAYGKnsssDLNDPEASIEAAAKY 59
 
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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