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CAZyme Information: MGYG000003582_00898

You are here: Home > Sequence: MGYG000003582_00898

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 Firm-07 sp900770145
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; Firm-07; Firm-07 sp900770145
CAZyme ID MGYG000003582_00898
CAZy Family GH23
CAZyme Description Soluble lytic murein transglycosylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
180 20166.19 6.9556
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003582 1806619 MAG Fiji Oceania
Gene Location Start: 301;  End: 843  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003582_00898.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 43 172 3.7e-31 0.8222222222222222

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16896 LT_Slt70-like 1.85e-60 27 167 3 145
uncharacterized lytic transglycosylase subfamily with similarity to Slt70. Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. 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.
cd13401 Slt70-like 1.65e-48 28 166 6 146
70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. 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. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
cd00254 LT-like 2.69e-40 45 166 3 110
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.
cd16893 LT_MltC_MltE 3.25e-29 30 166 1 161
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins. MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda
COG0741 MltE 3.83e-29 23 169 134 283
Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains) [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNK41497.1 1.65e-35 1 169 13 184
QAT49510.1 1.77e-34 27 169 40 182
QNU68364.1 1.77e-32 1 165 16 180
QKN24320.1 5.75e-32 28 175 61 214
QKO30667.1 5.75e-32 28 175 61 214

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FBT_A 1.72e-22 46 174 467 597
ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A 1.76e-22 46 174 496 626
TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
6FC4_A 4.37e-22 46 174 468 598
ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
6FCQ_A 4.37e-22 46 174 467 597
ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa],6FCR_A Chain A, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa],6FCS_A Chain A, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa],6FCU_A Chain A, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
1QSA_A 1.14e-17 28 173 453 601
CrystalStructure Of The 70 Kda Soluble Lytic Transglycosylase Slt70 From Escherichia Coli At 1.65 Angstroms Resolution [Escherichia coli],1QTE_A Crystal Structure Of The 70 Kda Soluble Lytic Transglycosylase Slt70 From Escherichia Coli At 1.90 A Resolution In Complex With A 1,6- Anhydromurotripeptide [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31608 4.15e-18 22 166 54 179
Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
P0AGC3 6.31e-17 28 173 480 628
Soluble lytic murein transglycosylase OS=Escherichia coli (strain K12) OX=83333 GN=slt PE=1 SV=1
P0AGC4 6.31e-17 28 173 480 628
Soluble lytic murein transglycosylase OS=Escherichia coli O157:H7 OX=83334 GN=slt PE=3 SV=1
P39434 5.43e-16 28 173 480 628
Soluble lytic murein transglycosylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=slt PE=3 SV=2
O31976 1.58e-15 27 166 1421 1541
SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000240 0.999154 0.000154 0.000157 0.000139 0.000132

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003582_00898.