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CAZyme Information: MGYG000002508_03179

You are here: Home > Sequence: MGYG000002508_03179

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 Hafnia alvei
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Hafnia; Hafnia alvei
CAZyme ID MGYG000002508_03179
CAZy Family GH102
CAZyme Description Membrane-bound lytic murein transglycosylase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
371 MGYG000002508_1|CGC28 41070.4 9.5897
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002508 4498956 Isolate South Korea Asia
Gene Location Start: 3451081;  End: 3452196  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002508_03179.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH102 126 260 1.5e-42 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 1 357 1 355
murein transglycosylase A; Provisional
COG2821 MltA 1.78e-166 1 366 1 373
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis].
smart00925 MltA 9.79e-64 125 260 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 1.65e-59 126 262 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 9.18e-55 126 262 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
QBJ34367.1 1.55e-276 1 371 1 371
AIU74024.1 1.55e-276 1 371 1 371
AMO80933.1 1.55e-276 1 371 1 371
ANC40894.1 1.55e-276 1 371 1 371
AWV45962.1 1.55e-276 1 371 1 371

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GAE_A 4.60e-186 20 367 1 345
Crystalstructure of MltA from E. coli [Escherichia coli]
2AE0_X 2.97e-184 22 367 2 344
Crystalstructure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold [Escherichia coli]
2PJJ_A 4.90e-183 22 367 2 344
ChainA, Membrane-bound lytic murein transglycosylase A [Escherichia coli K-12]
2PIC_A 9.87e-183 22 367 2 344
ChainA, Membrane-bound lytic murein transglycosylase A [Escherichia coli K-12]
2PI8_A 6.91e-176 22 367 2 344
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 1.85e-194 1 367 1 364
Membrane-bound lytic murein transglycosylase A OS=Escherichia coli (strain K12) OX=83333 GN=mltA PE=1 SV=1
P0A936 1.85e-194 1 367 1 364
Membrane-bound lytic murein transglycosylase A OS=Escherichia coli O157:H7 OX=83334 GN=mltA PE=3 SV=1
P57531 1.46e-117 27 356 28 356
Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=mltA PE=3 SV=1
Q8K9A7 7.89e-114 23 357 32 365
Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=mltA PE=3 SV=1
Q9KPQ4 8.21e-109 15 361 11 354
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 1.000078 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002508_03179.