lytic murein transglycosylase B is murein-degrading enzyme that catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases ...
96-390
1.53e-172
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274066 [Multi-domain] Cd Length: 290 Bit Score: 483.05 E-value: 1.53e-172
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
183-389
7.57e-30
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381602 [Multi-domain] Cd Length: 108 Bit Score: 111.25 E-value: 7.57e-30
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases ...
96-390
1.53e-172
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274066 [Multi-domain] Cd Length: 290 Bit Score: 483.05 E-value: 1.53e-172
lytic murein transglycosylase; Members of this family are closely related to the MltB family ...
107-391
1.67e-57
lytic murein transglycosylase; Members of this family are closely related to the MltB family lytic murein transglycosylases described by TIGR02282 and are likewise all proteobacterial, although that family and this one form clearly distinct clades. Several species have one member of each family. Many members of this family (unlike the MltB family) contain an additional C-terminal domain, a putative peptidoglycan binding domain (pfam01471), not included in region described by this model. Many sequences appear to contain N-terminal lipoprotein attachment sites, as does E. coli MltB in TIGR02282. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274067 [Multi-domain] Cd Length: 300 Bit Score: 189.90 E-value: 1.67e-57
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
183-389
7.57e-30
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381602 [Multi-domain] Cd Length: 108 Bit Score: 111.25 E-value: 7.57e-30
lysozyme-like domains; This family contains several members, including soluble lytic ...
235-294
1.09e-05
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: 42.78 E-value: 1.09e-05
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
251-316
3.53e-05
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
Pssm-ID: 381594 [Multi-domain] Cd Length: 111 Bit Score: 42.59 E-value: 3.53e-05
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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