bifunctional lytic transglycosylase/C40 family peptidase may catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and/or cleave peptide cross-bridges between glycan chains
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
68-228
2.24e-58
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to 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).
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Pssm-ID: 381612 [Multi-domain] Cd Length: 151 Bit Score: 186.27 E-value: 2.24e-58
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
68-228
2.24e-58
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to 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: 381612 [Multi-domain] Cd Length: 151 Bit Score: 186.27 E-value: 2.24e-58
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as ...
258-340
1.21e-08
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region.
Pssm-ID: 468486 [Multi-domain] Cd Length: 361 Bit Score: 56.28 E-value: 1.21e-08
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall ...
68-228
2.24e-58
CwlT-like N-terminal lysozyme domain and similar domains; CwlT is a bifunctional cell wall hydrolase containing an N-terminal lysozyme domain and a C-terminal NlpC/P60 endopeptidase domain (gamma-d-D-glutamyl-L-diamino acid endopeptidase), and has been implicated in the spread of transposons. Proteins similar to 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: 381612 [Multi-domain] Cd Length: 151 Bit Score: 186.27 E-value: 2.24e-58
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as ...
258-340
1.21e-08
peptidoglycan hydrolase RipC; RipC is a peptidoglycan hydrolase, found in species such as Mycobacterium tuberculosis, that is activated by conformation change sent as a signal by the cell division-regulating transporter-like complex FtsEX. Members of this family are distinguished from more distant homologs by a Pro/Gly-rich region.
Pssm-ID: 468486 [Multi-domain] Cd Length: 361 Bit Score: 56.28 E-value: 1.21e-08
Bacteriophage peptidoglycan hydrolase; At least one of the members of this family, the Pal ...
279-364
1.45e-05
Bacteriophage peptidoglycan hydrolase; At least one of the members of this family, the Pal protein from the pneumococcal bacteriophage Dp-1 has been shown to be a N-acetylmuramoyl-L-alanine amidase. According to the known modular structure of this and other peptidoglycan hydrolases from the pneumococcal system, the active site should reside at the N-terminal domain whereas the C-terminal domain binds to the choline residues of the cell wall teichoic acids. This family appears to be related to pfam00877.
Pssm-ID: 283125 Cd Length: 142 Bit Score: 44.52 E-value: 1.45e-05
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
86-181
3.03e-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: 3.03e-05
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
72-185
1.41e-03
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
Pssm-ID: 396169 [Multi-domain] Cd Length: 114 Bit Score: 38.06 E-value: 1.41e-03
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
281-340
4.02e-03
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.
Pssm-ID: 461605 [Multi-domain] Cd Length: 83 Bit Score: 35.86 E-value: 4.02e-03
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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