CAZyme Information: MGYG000002616_00124

Basic Information

• Species: CAG-495 sp001917125
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; RF32; CAG-239; CAG-495; CAG-495 sp001917125
• CAZyme ID: MGYG000002616_00124
• CAZy Family: GH102
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
405		45176.17	9.6006

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002616	1919079	MAG	China	Asia

• Gene Location: Start: 129863; End: 131080 Strand: -

Full Sequence      

MKKLFSLIVLSLLLASCGKEESSPKPQQVEELPQISIDKTPVPVTPPQPKIKLEARQFKD
LPNWKNDNLVEALSGFKHSCLKILKEKGPFLSDSELRIPTAAYQLACQRLINADISTAVE
FKYFLESNFLPFLVIADGSDQGKFTSYYEAAINASPIQTGIYKFPIYGKPLDLIEFNPRD
FDPSLPSKRLIGRVKDQKLIPYYTREEIEKNNISAPVILWGDSNIDINIMQIQGSAVATL
PDGRTVRISYADNNGHPFKGIGSILLEKGYIKPGEATMGNIKKWLKANPEIAAREMRENK
RFIFHRISRADGPIGAHGVPLHAGRSLAVDRRYIPLGSLIWLETTGPDREKIEKLVVAQD
IGSAIKGPIRGDYFWGSGKDDVLEKAGKMNSAGRYFILIPQNKAN

Enzyme Prediction     

No EC number prediction in MGYG000002616_00124.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH102	152	306	1.8e-46	0.9936305732484076

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG2821	MltA	1.57e-85	58	404	15	369	Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis].
pfam03562	MltA	7.69e-79	64	306	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	5.08e-67	152	307	1	158	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	4.67e-54	152	306	2	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	2.89e-42	276	398	27	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	4.00e-143	1	403	1	386
QBS11183.1	1.07e-79	48	405	6	370
AVM79582.1	4.41e-79	1	404	1	388
AVM75679.1	4.41e-79	1	404	1	388
QQP89444.1	1.17e-78	8	404	28	406

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7ESJ_A	9.32e-63	89	401	33	360	ChainA, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii],7ESJ_B Chain B, membrane-bound lytic murein transglycosylase A [Acinetobacter baumannii]
6QK4_B	3.66e-56	58	402	30	348	Lytictransglycosylase, LtgG, of Burkholderia pseudomallei. [Burkholderia pseudomallei]
2G5D_A	6.33e-55	61	400	50	413	Crystalstructure of MltA from Neisseria gonorrhoeae Monoclinic form [Neisseria gonorrhoeae FA 1090]
2G6G_A	7.38e-52	62	400	51	413	Crystalstructure of MltA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090]
2PNW_A	1.46e-44	58	401	14	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
P0A935	6.05e-23	136	398	110	353	Membrane-bound lytic murein transglycosylase A OS=Escherichia coli (strain K12) OX=83333 GN=mltA PE=1 SV=1
P0A936	6.05e-23	136	398	110	353	Membrane-bound lytic murein transglycosylase A OS=Escherichia coli O157:H7 OX=83334 GN=mltA PE=3 SV=1
P57531	4.34e-21	143	398	117	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	8.58e-19	54	395	42	355	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
0.000000	0.000000	1.000050	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002616_00124.