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CAZyme Information: MGYG000003393_01188

You are here: Home > Sequence: MGYG000003393_01188

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 Pantoea ananatis
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Pantoea; Pantoea ananatis
CAZyme ID MGYG000003393_01188
CAZy Family GH102
CAZyme Description Membrane-bound lytic murein transglycosylase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
382 42078.48 9.543
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003393 4793768 MAG United States North America
Gene Location Start: 436193;  End: 437341  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003393_01188.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH102 126 259 6.6e-41 0.9936305732484076

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK11162 mltA 0.0 1 356 1 355
murein transglycosylase A; Provisional
COG2821 MltA 9.62e-156 1 363 1 371
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis].
smart00925 MltA 3.56e-61 125 259 1 153
MltA specific insert domain. This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.
cd14472 mltA_B_like 3.76e-61 126 261 1 134
Domain B insert of mltA_like lytic transglycosylases. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.
cd14668 mlta_B 9.05e-56 126 261 1 159
Domain B insert of mltA_like lytic transglycosylases. Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QKV87898.1 7.84e-287 1 382 1 382
QTC47117.1 7.84e-287 1 382 1 382
QAB29284.1 7.84e-287 1 382 1 382
AMB76977.1 7.84e-287 1 382 1 382
ADD78269.1 8.45e-287 1 382 3 384

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GAE_A 4.49e-189 20 362 1 341
Crystalstructure of MltA from E. coli [Escherichia coli]
2AE0_X 2.90e-187 22 362 2 340
Crystalstructure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold [Escherichia coli]
2PJJ_A 4.78e-186 22 362 2 340
ChainA, Membrane-bound lytic murein transglycosylase A [Escherichia coli K-12]
2PIC_A 9.63e-186 22 362 2 340
ChainA, Membrane-bound lytic murein transglycosylase A [Escherichia coli K-12]
2PI8_A 1.66e-179 22 362 2 340
Crystalstructure of E. coli MltA with bound chitohexaose [Escherichia coli K-12],2PI8_B Crystal structure of E. coli MltA with bound chitohexaose [Escherichia coli K-12],2PI8_C Crystal structure of E. coli MltA with bound chitohexaose [Escherichia coli K-12],2PI8_D Crystal structure of E. coli MltA with bound chitohexaose [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0A935 1.55e-198 1 362 1 360
Membrane-bound lytic murein transglycosylase A OS=Escherichia coli (strain K12) OX=83333 GN=mltA PE=1 SV=1
P0A936 1.55e-198 1 362 1 360
Membrane-bound lytic murein transglycosylase A OS=Escherichia coli O157:H7 OX=83334 GN=mltA PE=3 SV=1
P57531 4.09e-120 27 356 28 357
Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=mltA PE=3 SV=1
Q8K9A7 9.39e-113 24 356 33 365
Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=mltA PE=3 SV=1
Q9KPQ4 7.76e-99 6 355 2 349
Membrane-bound lytic murein transglycosylase A OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=mltA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000070 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003393_01188.