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Conserved domains on  [gi|486203748|ref|WP_001551053|]
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MULTISPECIES: lysozyme RrrD [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

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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 ...
 23-161 3.84e-82

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: 238.61  E-value: 3.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  23 VLITGPSGNDGLEGVSYIPYKDIVGVWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKVDIPETTRGAL 102
Cdd:cd16900    4 LALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQRAAL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 486203748 103 YSFVYNVGAGNFRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICL 161
Cdd:cd16900   84 ASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 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 ...
 23-161 3.84e-82

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: 238.61  E-value: 3.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  23 VLITGPSGNDGLEGVSYIPYKDIVGVWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKVDIPETTRGAL 102
Cdd:cd16900    4 LALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQRAAL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 486203748 103 YSFVYNVGAGNFRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICL 161
Cdd:cd16900   84 ASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
35-165 3.37e-70

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 208.54  E-value: 3.37e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  35 EGVSYIPYKDIVGVWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKVDIPETTRGALYSFVYNVGAGNF 114
Cdd:COG3772   16 EGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFAYNVGAGAF 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 486203748 115 RTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICLWGQQ 165
Cdd:COG3772   96 CRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 48-154 3.14e-38

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 126.31  E-value: 3.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748   48 VWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKV-DIPETTRGALYSFVYNVGAGNFRTSTLLRKINQG 126
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVkDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 486203748  127 DIKGACDQLRRWTYAgGKQWKGLMTRRE 154
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 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 ...
 23-161 3.84e-82

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: 238.61  E-value: 3.84e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  23 VLITGPSGNDGLEGVSYIPYKDIVGVWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKVDIPETTRGAL 102
Cdd:cd16900    4 LALAAAALVGPWEGLRLTAYRDPVGVWTVCYGHTGGDVKPGMRYTPAECDALLAKDLQEAAAAVDRCVKVPLPDPQRAAL 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 486203748 103 YSFVYNVGAGNFRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICL 161
Cdd:cd16900   84 ASFAYNVGVGAFCRSTLLRKLNAGDRRGACDELTRWVYAGGRVLRGLVNRREAERALCL 142
RrrD COG3772
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis];
35-165 3.37e-70

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


Pssm-ID: 442986 [Multi-domain]  Cd Length: 146  Bit Score: 208.54  E-value: 3.37e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  35 EGVSYIPYKDIVGVWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKVDIPETTRGALYSFVYNVGAGNF 114
Cdd:COG3772   16 EGFRLKAYRDPAGVWTIGYGHTGKDVKPGDTITEEEAEALLAADLAKAEAAVRRLVKVPLTQNQFDALVSFAYNVGAGAF 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 486203748 115 RTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICLWGQQ 165
Cdd:COG3772   96 CRSTLLRKLNAGDYAGACDELLRWVYAGGKVLPGLVRRREAERALCLGGLY 146
lyz_endolysin_autolysin cd00737
endolysin and autolysin; The dsDNA phages of eubacteria use endolysins or muralytic enzymes in ...
 35-161 4.32e-56

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: 172.32  E-value: 4.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  35 EGVSYIPYKDIVGVWTVCHGHTGKDII-PGKTYTEAECKALLNKDLATVARQINPYIKVDIPETTRGALYSFVYNVGAGN 113
Cdd:cd00737    9 EGLRLKAYRDPAGVWTIGYGHTGGVVVkPGDTITEAQAEALLRQDLARFEAAVNRLVKVPLNQNQFDALVSFAFNVGAGA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 486203748 114 FRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICL 161
Cdd:cd00737   89 FKSSTLLRKLNAGDYAGAADEFLRWNKAGGKVLPGLVRRRAAEAALFL 136
lyz_P1 cd16901
P1 lysozyme Lyz-like proteins; Enterobacteria phage P1 lysozyme Lyz is secreted to the ...
 35-161 3.13e-40

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: 132.35  E-value: 3.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  35 EGVSYIPYKDIVGVWTVCHGHTGKdIIPGKTYTEAECKALLNKDLATVARQINPYI-KVDIPETTRGALYSFVYNVGAGN 113
Cdd:cd16901   14 EGCRRDPYKCPAGVPTIGIGSTHG-VKPGDRYTDEQAAKRLAKDIKKAERCVNRCFnGVPLPQGEFDAYVSFAFNVGCGA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 486203748 114 FRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREICL 161
Cdd:cd16901   93 FCKSTIYKKLQAGDYAAACNQLPRWVYAGGKVLPGLVTRRQKERALCL 140
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 48-154 3.14e-38

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


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 126.31  E-value: 3.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748   48 VWTVCHGHTGKDIIPGKTYTEAECKALLNKDLATVARQINPYIKV-DIPETTRGALYSFVYNVGAGNFRTSTLLRKINQG 126
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRATKSEAAGRLQIDLDTAERCINQYHKVkDFNPNQQDALVSLAFNVGCGKRGFSTLLRAGNIG 80

                          90       100
                  ....*....|....*....|....*...
gi 486203748  127 DIKGACDQLRRWTYAgGKQWKGLMTRRE 154
Cdd:pfam00959  81 QWIKACSAIWKSLKA-GKVYNGLVNRRE 107
T4-like_lys cd00735
bacteriophage T4-like lysozymes; Bacteriophage T4-like lysozymes hydrolyze the beta-1, ...
 35-153 1.24e-14

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: 67.01  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486203748  35 EGVSYIPYKDIVGVWTVCHGHT---GKDIIPGKTYTEAECKALLNKDLATVARQI--NPYIK---VDIPETTRGALYSFV 106
Cdd:cd00735   10 EGYRLKAYKDTEGYPTIGIGHLigkKGASLTNGTITKDEAEALFEQDVDRAVRDMlrNPKLApvyAQLNAARRMALINMA 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 486203748 107 YNVGAGN---FRTStlLRKINQGDIKGACDQLRRwtYAGGKQWKGLMTRR 153
Cdd:cd00735   90 FQMGVGGlakFKNM--LAAIKAGDWEEAADGMLN--SLWAKQTPNRANRV 135
 
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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