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CAZyme Information: MGYG000004476_01512

You are here: Home > Sequence: MGYG000004476_01512

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
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA1259;
CAZyme ID MGYG000004476_01512
CAZy Family GH23
CAZyme Description Membrane-bound lytic murein transglycosylase C
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
201 MGYG000004476_39|CGC1 23203.71 7.639
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004476 1651123 MAG Israel Asia
Gene Location Start: 398;  End: 1003  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004476_01512.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH23 64 185 1.7e-27 0.7777777777777778

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16896 LT_Slt70-like 2.33e-56 44 179 1 140
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 7.54e-44 42 189 1 152
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.
381594 cd00254 1.70e-27 62 184 1 111
LT-like 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.
COG0741 MltE 2.84e-27 37 192 129 289
Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains) [Cell wall/membrane/envelope biogenesis].
cd16893 LT_MltC_MltE 6.92e-22 51 131 3 89
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

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACL76418.1 2.21e-45 40 190 37 191
AEY66639.1 8.89e-45 40 190 37 191
SLK19900.1 1.17e-44 39 192 25 181
ATD56881.1 1.17e-44 39 192 25 181
QBJ75740.1 1.17e-44 39 192 25 181

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FBT_A 2.05e-19 43 195 445 597
ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A 2.08e-19 43 195 474 626
TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
1QSA_A 3.80e-19 33 186 441 600
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]
6FCQ_A 5.15e-19 43 195 445 597
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]
6FC4_A 5.15e-19 43 195 446 598
ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0AGC4 2.11e-18 33 186 468 627
Soluble lytic murein transglycosylase OS=Escherichia coli O157:H7 OX=83334 GN=slt PE=3 SV=1
P0AGC3 2.11e-18 33 186 468 627
Soluble lytic murein transglycosylase OS=Escherichia coli (strain K12) OX=83333 GN=slt PE=1 SV=1
O31608 7.17e-18 55 179 68 175
Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
P39434 8.32e-17 33 179 468 618
Soluble lytic murein transglycosylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=slt PE=3 SV=2
O31976 2.33e-12 43 185 1418 1543
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
1.000043 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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