Species | Lactobacillus paragasseri | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus paragasseri | |||||||||||
CAZyme ID | MGYG000002387_00757 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 727675; End: 730089 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 50 | 235 | 2.8e-40 | 0.9717514124293786 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06415 | GH25_Cpl1-like | 1.37e-85 | 47 | 246 | 1 | 196 | Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage. |
cd00599 | GH25_muramidase | 3.77e-26 | 49 | 245 | 2 | 183 | Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity. |
pfam01183 | Glyco_hydro_25 | 4.84e-25 | 50 | 233 | 1 | 174 | Glycosyl hydrolases family 25. |
cd06522 | GH25_AtlA-like | 6.04e-25 | 50 | 245 | 4 | 188 | AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain. |
cd06414 | GH25_LytC-like | 1.90e-17 | 49 | 243 | 3 | 189 | The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QTP19769.1 | 0.0 | 1 | 804 | 1 | 804 |
ART98082.1 | 0.0 | 1 | 804 | 1 | 804 |
QHC52436.1 | 0.0 | 1 | 804 | 1 | 804 |
BBD47809.1 | 0.0 | 1 | 804 | 1 | 792 |
QTH65586.1 | 0.0 | 1 | 804 | 1 | 905 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1H09_A | 4.15e-22 | 50 | 239 | 8 | 184 | ChainA, LYSOZYME [Streptococcus phage Cp1] |
2IXU_A | 4.21e-22 | 50 | 239 | 9 | 185 | ChainA, LYSOZYME [Streptococcus phage Cp1] |
2IXV_A | 1.03e-21 | 50 | 239 | 9 | 185 | ChainA, LYSOZYME [Streptococcus phage Cp1],2J8F_A Chain A, LYSOZYME [Streptococcus phage Cp1],2J8G_A Chain A, LYSOZYME [Streptococcus phage Cp1] |
1OBA_A | 6.15e-21 | 50 | 239 | 9 | 185 | ChainA, Lysozyme [Streptococcus phage Cp1] |
6AKV_A | 5.64e-11 | 404 | 478 | 203 | 282 | ChainA, LysB4 [Bacillus phage B4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8HA43 | 6.06e-22 | 31 | 246 | 136 | 343 | D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2 |
P33486 | 6.69e-22 | 46 | 219 | 3 | 176 | Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3 |
P19386 | 1.71e-21 | 50 | 239 | 9 | 185 | Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1 |
P15057 | 2.31e-21 | 50 | 239 | 9 | 185 | Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 SV=2 |
P19385 | 2.24e-18 | 50 | 239 | 9 | 185 | Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000396 | 0.998810 | 0.000244 | 0.000204 | 0.000157 | 0.000137 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.