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CAZyme Information: MGYG000001894_01645

You are here: Home > Sequence: MGYG000001894_01645

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; Proteobacteria; Alphaproteobacteria; RF32; CAG-239; CAG-495;
CAZyme ID MGYG000001894_01645
CAZy Family GH102
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
385 43138.57 8.8914
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001894 1739362 MAG Denmark Europe
Gene Location Start: 743;  End: 1900  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001894_01645.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH102 130 284 7e-49 0.9936305732484076

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG2821 MltA 4.32e-90 100 381 81 368
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis].
pfam03562 MltA 1.20e-76 45 284 1 231
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.
cd14668 mlta_B 7.09e-66 130 286 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.
smart00925 MltA 4.20e-54 129 284 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.
cd14485 mltA_like_LT_A 2.98e-40 296 376 76 159
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B. 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
QJR98168.1 3.30e-149 8 379 5 384
QEX19872.1 1.04e-87 13 379 18 392
QEX25089.1 1.85e-86 13 384 23 401
ARH00321.1 1.47e-85 34 380 37 393
ARG97371.1 4.15e-85 34 380 37 393

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7ESJ_A 6.29e-61 99 383 78 364
ChainA, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii],7ESJ_B Chain B, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii]
2G5D_A 4.56e-57 72 382 67 417
Crystalstructure of MltA from Neisseria gonorrhoeae Monoclinic form [Neisseria gonorrhoeae FA 1090]
2G6G_A 2.97e-53 72 378 67 413
Crystalstructure of MltA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090]
6QK4_B 6.09e-51 44 380 35 348
Lytictransglycosylase, LtgG, of Burkholderia pseudomallei. [Burkholderia pseudomallei]
2PNW_A 8.74e-46 39 379 14 364
Crystalstructure of membrane-bound lytic murein transglycosylase from Agrobacterium tumefaciens [Agrobacterium fabrum str. C58]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P57531 1.22e-23 63 379 52 359
Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=mltA PE=3 SV=1
P0A935 1.06e-21 115 376 111 353
Membrane-bound lytic murein transglycosylase A OS=Escherichia coli (strain K12) OX=83333 GN=mltA PE=1 SV=1
P0A936 1.06e-21 115 376 111 353
Membrane-bound lytic murein transglycosylase A OS=Escherichia coli O157:H7 OX=83334 GN=mltA PE=3 SV=1
Q8K9A7 5.05e-21 62 376 59 364
Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=mltA PE=3 SV=1
Q9KPQ4 1.10e-17 115 344 106 319
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 0.000003 1.000037 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001894_01645.