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CAZyme Information: MGYG000000096_00131

You are here: Home > Sequence: MGYG000000096_00131

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Leuconostoc pseudomesenteroides
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Leuconostoc; Leuconostoc pseudomesenteroides
CAZyme ID MGYG000000096_00131
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
307 MGYG000000096_1|CGC2 33965.05 7.435
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000096 2296803 Isolate Canada North America
Gene Location Start: 132944;  End: 133867  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000096_00131.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 10 163 1.2e-29 0.807909604519774

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06415 GH25_Cpl1-like 1.98e-67 15 174 35 196
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.
pfam01183 Glyco_hydro_25 4.74e-21 15 163 33 174
Glycosyl hydrolases family 25.
smart00641 Glyco_25 3.75e-16 67 171 1 100
Glycosyl hydrolases family 25.
cd06414 GH25_LytC-like 2.53e-13 15 171 39 185
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.
cd00599 GH25_muramidase 1.58e-12 15 171 35 181
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQB26664.1 7.09e-204 1 307 57 363
ADP69243.1 7.09e-204 1 307 57 363
ARR89695.1 1.59e-200 1 307 57 363
QHJ81406.1 1.59e-200 1 307 57 363
AHF19626.1 6.17e-198 1 307 57 363

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1H09_A 1.62e-25 11 182 36 195
ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXU_A 1.64e-25 11 182 37 196
ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXV_A 4.35e-25 11 182 37 196
ChainA, LYSOZYME [Streptococcus phage Cp1],2J8F_A Chain A, LYSOZYME [Streptococcus phage Cp1],2J8G_A Chain A, LYSOZYME [Streptococcus phage Cp1]
1OBA_A 3.02e-24 11 182 37 196
ChainA, Lysozyme [Streptococcus phage Cp1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P15057 9.00e-25 11 182 37 196
Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 SV=2
P19386 8.28e-23 11 182 37 196
Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 PE=3 SV=1
P19385 1.64e-22 11 181 37 192
Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2
Q8HA43 2.53e-20 15 174 189 343
D-alanyl-L-alanine endopeptidase OS=Streptococcus phage B30 OX=209152 PE=1 SV=2
P33486 1.54e-15 43 149 66 176
Lysozyme OS=Lactococcus phage mv1 OX=33769 GN=lysA PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000049 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000096_00131.