CAZyme Information: MGYG000003827_01208

Basic Information

• Species: 51-20 sp900539605
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; RF32; CAG-239; 51-20; 51-20 sp900539605
• CAZyme ID: MGYG000003827_01208
• CAZy Family: GH102
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
384		43123.83	6.3993

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003827	1662387	MAG	United States	North America

• Gene Location: Start: 9377; End: 10531 Strand: +

Full Sequence      

MVVFLLAGCPSRQEKQPLPAERTAAEKVELTPVSFHELENWQDDDLTQFVEVFAATCAKI
RQLKTPYLADSQIKIKTADYQEICRRFDEEGIGNGQELRIFFETYFTPYLVQGNGNADGK
FTSYYEAEIRASRQRHGKYRYPVYGKPHNLIEINLRDFDPDLPDARLVGRISGQKMLPYY
TRADIEKAPFNAPVLLWGDSAVDIHIMQIQGSAIARLDDGSQVRIGYADNNGRRFKGIGG
ILLGKGLLEAGKTDMMSIKKWLEENPQQATAIMQENERYIFHRFITTSGPVGAFGIPLTA
GRSLAVDRRYIPLGAILWLSTTTPDHQPLNKMVAAQDIGSAIKGAVRGDYFWGSGGDEIL
NSAGRMNSSGHYYIFLPRENNNDE

Enzyme Prediction     

No EC number prediction in MGYG000003827_01208.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH102	129	283	2.6e-49	0.9936305732484076

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG2821	MltA	5.20e-77	30	378	10	366	Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis].
pfam03562	MltA	1.60e-71	41	283	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	1.47e-55	129	285	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	2.90e-45	128	283	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	2.42e-39	258	375	32	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJR98168.1	6.15e-159	1	378	7	384
CUW37894.1	1.47e-90	6	378	14	380
ARJ66419.1	5.87e-90	6	378	14	380
BAE53346.1	3.61e-87	26	378	32	378
QEX19872.1	8.96e-86	1	378	15	392

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6QK4_B	2.59e-65	8	377	1	346	Lytictransglycosylase, LtgG, of Burkholderia pseudomallei. [Burkholderia pseudomallei]
7ESJ_A	1.19e-64	54	378	21	360	ChainA, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii],7ESJ_B Chain B, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii]
2G5D_A	1.56e-62	10	377	21	413	Crystalstructure of MltA from Neisseria gonorrhoeae Monoclinic form [Neisseria gonorrhoeae FA 1090]
2G6G_A	1.96e-59	10	377	21	413	Crystalstructure of MltA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090]
2PNW_A	1.19e-45	33	378	12	364	Crystalstructure of membrane-bound lytic murein transglycosylase from Agrobacterium tumefaciens [Agrobacterium fabrum str. C58]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P57531	1.38e-19	94	344	93	327	Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=mltA PE=3 SV=1
P0A935	1.44e-17	89	374	85	352	Membrane-bound lytic murein transglycosylase A OS=Escherichia coli (strain K12) OX=83333 GN=mltA PE=1 SV=1
P0A936	1.44e-17	89	374	85	352	Membrane-bound lytic murein transglycosylase A OS=Escherichia coli O157:H7 OX=83334 GN=mltA PE=3 SV=1
Q8K9A7	6.36e-14	97	374	104	363	Membrane-bound lytic murein transglycosylase A homolog OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=mltA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.144665	0.003159	0.852207	0.000005	0.000008	0.000005

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003827_01208.