CAZyme Information: MGYG000000445_00471

Basic Information

• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; RF32; CAG-239; RUG410
• CAZyme ID: MGYG000000445_00471
• CAZy Family: GH102
• CAZyme Description: Membrane-bound lytic murein transglycosylase A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
402		44905.87	9.4991

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000445	1525621	MAG	Sweden	Europe

• Gene Location: Start: 9137; End: 10345 Strand: -

Full Sequence      

MQKTITGCWFPLKKRLNFVLSLVLLLLLSGCFSEEPKIPSAEESKVVLKKIGFNRLPGWN
ADDFGEVIPVFAKNCQNVLKNKNAYLYNSAIKIKTSDYQKVCKKFANAGINSGAQMKKFM
ENEFAPYMVSDDGKADGKFTSYYEATIYASFEKSAKYKFPIYGKPNDLIEINLKDFDSAL
PNTRLVGRVEGKKFIPYYDRRQIEQNGVKAPVLMWGDDLVDIHFMQIQGSAIAIMDDGSE
LRIGFADSNGRKFKGIGSILLQKGLIKPGEASMTKIRDWLRKNPQKAAEVMAENERFIFQ
RVVDADGPVGAYGLSLTAGRSMAVDNKYIPLGAVLWLDTVNPDREKIEKVVFAQDIGSAI
KGVVRGDYFWGHGEEALAEAGRMNSVGKYYLLAPKYSAPKVD

Enzyme Prediction     

No EC number prediction in MGYG000000445_00471.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH102	148	299	2.8e-49	0.9745222929936306

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG2821	MltA	6.95e-88	56	401	18	372	Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis].
pfam03562	MltA	2.84e-87	59	299	1	229	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	7.21e-71	149	299	3	155	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	1.98e-58	146	299	1	151	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	4.21e-40	275	392	31	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	7.20e-143	23	402	7	391
AMW34438.1	7.81e-96	23	399	16	381
QQP89444.1	7.04e-89	21	399	27	407
CUW37894.1	9.47e-88	21	401	7	386
AVM79582.1	6.57e-87	22	401	8	391

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2G5D_A	4.09e-65	56	400	50	419	Crystalstructure of MltA from Neisseria gonorrhoeae Monoclinic form [Neisseria gonorrhoeae FA 1090]
7ESJ_A	6.09e-63	98	395	60	360	ChainA, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii],7ESJ_B Chain B, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii]
2G6G_A	5.16e-62	57	400	51	419	Crystalstructure of MltA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090]
6QK4_B	2.99e-53	48	394	25	346	Lytictransglycosylase, LtgG, of Burkholderia pseudomallei. [Burkholderia pseudomallei]
3CZB_A	2.24e-48	51	394	10	341	Crystalstructure of putative transglycosylase from Caulobacter crescentus [Caulobacter vibrioides CB15],3CZB_B Crystal structure of putative transglycosylase from Caulobacter crescentus [Caulobacter vibrioides CB15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P57531	1.24e-19	107	395	91	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	7.70e-17	60	392	55	353	Membrane-bound lytic murein transglycosylase A OS=Escherichia coli (strain K12) OX=83333 GN=mltA PE=1 SV=1
P0A936	7.70e-17	60	392	55	353	Membrane-bound lytic murein transglycosylase A OS=Escherichia coli O157:H7 OX=83334 GN=mltA PE=3 SV=1
Q9KPQ4	7.72e-13	132	392	106	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

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000156	0.001766	0.998070	0.000023	0.000006	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000445_00471.