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CAZyme Information: MGYG000002903_00513

You are here: Home > Sequence: MGYG000002903_00513

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 Negativicoccus succinicivorans
Lineage Bacteria; Firmicutes_C; Negativicutes; Veillonellales; Negativicoccaceae; Negativicoccus; Negativicoccus succinicivorans
CAZyme ID MGYG000002903_00513
CAZy Family GH23
CAZyme Description Membrane-bound lytic murein transglycosylase F
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
188 22107.94 5.7742
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002903 1204906 MAG United States North America
Gene Location Start: 8721;  End: 9287  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002903_00513.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 49 173 3.5e-31 0.8

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16896 LT_Slt70-like 5.44e-67 36 172 4 144
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 3.97e-52 36 176 6 150
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 7.48e-40 51 173 1 111
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.
cd13403 MLTF-like 5.37e-35 43 142 4 104
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins. This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase 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, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
pfam01464 SLT 4.35e-33 43 146 4 108
Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SNV63004.1 6.06e-42 1 181 1 182
AIF51128.1 7.02e-42 20 179 24 187
BBK24355.1 1.58e-41 33 169 48 185
CAB1276067.1 6.90e-41 1 175 1 176
QDR80996.1 7.98e-41 4 179 2 187

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1SLY_A 7.59e-22 34 175 451 598
ComplexOf The 70-Kda Soluble Lytic Transglycosylase With Bulgecin A [Escherichia coli]
1QSA_A 7.59e-22 34 175 451 598
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]
6FBT_A 3.07e-16 44 177 457 594
ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A 3.11e-16 44 177 486 623
TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
5MPQ_A 7.58e-16 43 179 423 559
BulgecinA: The key to a broad-spectrum inhibitor that targets lytic transglycosylases [Neisseria meningitidis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0AGC3 4.22e-21 34 175 478 625
Soluble lytic murein transglycosylase OS=Escherichia coli (strain K12) OX=83333 GN=slt PE=1 SV=1
P0AGC4 4.22e-21 34 175 478 625
Soluble lytic murein transglycosylase OS=Escherichia coli O157:H7 OX=83334 GN=slt PE=3 SV=1
P39434 1.45e-20 34 178 478 628
Soluble lytic murein transglycosylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=slt PE=3 SV=2
O31608 1.42e-17 35 168 59 175
Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O31976 1.99e-15 35 169 1421 1538
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.885509 0.097305 0.013224 0.000545 0.000296 0.003143

TMHMM  Annotations      download full data without filtering help

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