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Conserved domains on  [gi|60594002|pdb|1XJU|B]
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Chain B, Lysozyme

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 ...
 1-151 6.46e-79

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: 230.19  E-value: 6.46e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        1 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSA 80
Cdd:cd16901   1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1XJU_B       81 MTSAAFNMGCNSLRtyyskargmrvETSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 151
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 ...
 1-151 6.46e-79

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: 230.19  E-value: 6.46e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        1 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSA 80
Cdd:cd16901   1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1XJU_B       81 MTSAAFNMGCNSLRtyyskargmrvETSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 151
Cdd:cd16901  81 YVSFAFNVGCGAFC-----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
1-154 6.81e-48

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 151.92  E-value: 6.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        1 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNT-HGVTPGVRKTDQQIAADWEKNILIAERCINQHFrGKDMPDNAFS 79
Cdd:COG3772   3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQNQFD 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1XJU_B       80 AMTSAAFNMGCNSLRTyyskargmrveTSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCLTGL 154
Cdd:COG3772  82 ALVSFAYNVGAGAFCR-----------STLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 27-144 8.69e-36

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 120.15  E-value: 8.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B         27 VWTDGIG-NTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSAMTSAAFNMGCnslrtyyskarGMRV 105
Cdd:pfam00959   1 YWTIGIGhNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGC-----------GKRG 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
1XJU_B        106 ETSIHKWAQKGEWVNMCNHLPDFVNSnGVPLRGLKIRRE 144
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 ...
 1-151 6.46e-79

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: 230.19  E-value: 6.46e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        1 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSA 80
Cdd:cd16901   1 RTSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFNGVPLPQGEFDA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1XJU_B       81 MTSAAFNMGCNSLRtyyskargmrvETSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 151
Cdd:cd16901  81 YVSFAFNVGCGAFC-----------KSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
1-154 6.81e-48

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 151.92  E-value: 6.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        1 RTNQAGLELIGNAEGCRRDPYMCPAGVWTDGIGNT-HGVTPGVRKTDQQIAADWEKNILIAERCINQHFrGKDMPDNAFS 79
Cdd:COG3772   3 KTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLV-KVPLTQNQFD 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1XJU_B       80 AMTSAAFNMGCNSLRTyyskargmrveTSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCLTGL 154
Cdd:COG3772  82 ALVSFAYNVGAGAFCR-----------STLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 6-151 1.63e-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: 1.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        6 GLELIGNAEGCRRDPYMCPAGVWTDGIGNTHGV--TPGVRKTDQQIAADWEKNILIAERCINQHFRgKDMPDNAFSAMTS 83
Cdd:cd00737   1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTGGVvvKPGDTITEAQAEALLRQDLARFEAAVNRLVK-VPLNQNQFDALVS 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1XJU_B       84 AAFNMGCNSLRTyyskargmrveTSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 151
Cdd:cd00737  80 FAFNVGAGAFKS-----------STLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 27-144 8.69e-36

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 120.15  E-value: 8.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B         27 VWTDGIG-NTHGVTPGVRKTDQQIAADWEKNILIAERCINQHFRGKDMPDNAFSAMTSAAFNMGCnslrtyyskarGMRV 105
Cdd:pfam00959   1 YWTIGIGhNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVKDFNPNQQDALVSLAFNVGC-----------GKRG 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
1XJU_B        106 ETSIHKWAQKGEWVNMCNHLPDFVNSnGVPLRGLKIRRE 144
Cdd:pfam00959  70 FSTLLRAGNIGQWIKACSAIWKSLKA-GKVYNGLVNRRE 107
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 9-151 1.13e-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: 71.82  E-value: 1.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        9 LIGNAEGCRRDPYMCPAGVWT--DGIgnTHG-VTPGVRKTDQQIAADWEKNILIAERCINQHFRGkDMPDNAFSAMTSAA 85
Cdd:cd16900  11 LVGPWEGLRLTAYRDPVGVWTvcYGH--TGGdVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKV-PLPDPQRAALASFA 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B       86 FNMG----CNSlrtyyskargmrvetSIHKWAQKGEWVNMCNHLPDFVNSNGVPLRGLKIRREKERQLCL 151
Cdd:cd16900  88 YNVGvgafCRS---------------TLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
chitinase-like cd16889
chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, ...
 6-87 1.54e-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: 70.68  E-value: 1.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1XJU_B        6 GLELIGNAEGCRRDPY-----MCPAGVWTDGIGNTHGVTPG----------------VRKTDQQIAADWEKNILIAERCI 64
Cdd:cd16889   1 WFLLITSLETKGLGPTavygdGKDPRGYTRGIGVTHGMLRGstsrfpgvdtsnqtnnGASTDSQLAKLAMEGFDPAYRAL 80

                        90       100
                ....*....|....*....|....*
1XJU_B       65 NQHF--RGKDMPDNAFSAMTSAAFN 87
Cdd:cd16889  81 MRTIahRDDLSPHVNGCAVIFAGFN 105
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 6-59 7.11e-04

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: 36.23  E-value: 7.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
1XJU_B        6 GLELIGNAEGCRRDPYMCPAGVWTDGIG-NTHGVTPGVRK----TDQQIAADWEKNILI 59
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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