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Conserved domains on  [gi|1997187516|ref|WP_205952316|]
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lysozyme [Pantoea stewartii]

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 ...
 28-165 7.49e-59

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: 179.72  E-value: 7.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  28 TSEAGLRLIADAEGCRTSPYQCSAGVWTNGIGHTQGVTPASVVNERQAAVNLVYDVMRVERGIDLCM-TRDMPSEVYDAV 106
Cdd:cd16901     2 TSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFnGVPLPQGEFDAY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1997187516 107 VSFGFNVGVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMAWCL 165
Cdd:cd16901    82 VSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 28-165 7.49e-59

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: 179.72  E-value: 7.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  28 TSEAGLRLIADAEGCRTSPYQCSAGVWTNGIGHTQGVTPASVVNERQAAVNLVYDVMRVERGIDLCM-TRDMPSEVYDAV 106
Cdd:cd16901     2 TSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFnGVPLPQGEFDAY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1997187516 107 VSFGFNVGVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMAWCL 165
Cdd:cd16901    82 VSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
25-168 2.09e-57

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 176.18  E-value: 2.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  25 MLKTSEAGLRLIADAEGCRTSPYQCSAGVWTNGIGHT-QGVTPASVVNERQAAVNLVYDVMRVERGIDLCMTRDMPSEVY 103
Cdd:COG3772     1 MMKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997187516 104 DAVVSFGFNVGVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMAWCLKGA 168
Cdd:COG3772    81 DALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 53-158 4.72e-14

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 64.30  E-value: 4.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  53 VWTNGIGH-TQGVTPASVVNERQAAVNLVYDVMRVERGID-LCMTRDMPSEVYDAVVSFGFNVGVHAACNSTLAGFINRG 130
Cdd:pfam00959   1 YWTIGIGHnGKDVSPHPRATKSEAAGRLQIDLDTAERCINqYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 1997187516 131 RWRDACLQLRRWVYVKGTYNaGLDNRRQ 158
Cdd:pfam00959  81 QWIKACSAIWKSLKAGKVYN-GLVNRRE 107
 
Name Accession Description Interval E-value
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 28-165 7.49e-59

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: 179.72  E-value: 7.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  28 TSEAGLRLIADAEGCRTSPYQCSAGVWTNGIGHTQGVTPASVVNERQAAVNLVYDVMRVERGIDLCM-TRDMPSEVYDAV 106
Cdd:cd16901     2 TSAAGLELIANAEGCRRDPYKCPAGVPTIGIGSTHGVKPGDRYTDEQAAKRLAKDIKKAERCVNRCFnGVPLPQGEFDAY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1997187516 107 VSFGFNVGVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMAWCL 165
Cdd:cd16901    82 VSFAFNVGCGAFCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
25-168 2.09e-57

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 176.18  E-value: 2.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  25 MLKTSEAGLRLIADAEGCRTSPYQCSAGVWTNGIGHT-QGVTPASVVNERQAAVNLVYDVMRVERGIDLCMTRDMPSEVY 103
Cdd:COG3772     1 MMKTSAAGLALIKEFEGFRLKAYRDPAGVWTIGYGHTgKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1997187516 104 DAVVSFGFNVGVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMAWCLKGA 168
Cdd:COG3772    81 DALVSFAYNVGAGAFCRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGL 145
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 32-162 1.88e-39

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: 130.33  E-value: 1.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  32 GLRLIADAEGCRTSPYQCSAGVWTNGIGHT--QGVTPASVVNERQAAVNLVYDVMRVERGIDLCMTRDMPSEVYDAVVSF 109
Cdd:cd00737     1 GLDLIKEFEGLRLKAYRDPAGVWTIGYGHTggVVVKPGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1997187516 110 GFNVGVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMA 162
Cdd:cd00737    81 AFNVGAGAFKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAA 133
endolysin_R21-like cd16900
endolysin R21-like proteins; Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria ...
 35-165 1.11e-31

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: 110.72  E-value: 1.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  35 LIADAEGCRTSPYQCSAGVWTNGIGHTQG-VTPASVVNERQAAVNLVYDVMRVERGIDLCMTRDMPSEVYDAVVSFGFNV 113
Cdd:cd16900    11 LVGPWEGLRLTAYRDPVGVWTVCYGHTGGdVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQRAALASFAYNV 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1997187516 114 GVHAACNSTLAGFINRGRWRDACLQLRRWVYVKGTYNAGLDNRRQREMAWCL 165
Cdd:cd16900    91 GVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 53-158 4.72e-14

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 64.30  E-value: 4.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  53 VWTNGIGH-TQGVTPASVVNERQAAVNLVYDVMRVERGID-LCMTRDMPSEVYDAVVSFGFNVGVHAACNSTLAGFINRG 130
Cdd:pfam00959   1 YWTIGIGHnGKDVSPHPRATKSEAAGRLQIDLDTAERCINqYHKVKDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 1997187516 131 RWRDACLQLRRWVYVKGTYNaGLDNRRQ 158
Cdd:pfam00959  81 QWIKACSAIWKSLKAGKVYN-GLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 40-150 7.03e-07

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: 46.21  E-value: 7.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1997187516  40 EGCRTSPYQCSAGVWTNGIGHTQGVTPASVVNER----QAAVNLVYDVMRVERGIDLCMTrdmPSEVY--------DAVV 107
Cdd:cd00735    10 EGYRLKAYKDTEGYPTIGIGHLIGKKGASLTNGTitkdEAEALFEQDVDRAVRDMLRNPK---LAPVYaqlnaarrMALI 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1997187516 108 SFGFNVGVHAAC--NSTLAgFINRGRWRDACLQLRRWVYVKGTYN 150
Cdd:cd00735    87 NMAFQMGVGGLAkfKNMLA-AIKAGDWEEAADGMLNSLWAKQTPN 130
 
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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