CAZyme Information: MGYG000000014_04138

Basic Information

• Species: Clostridium butyricum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum
• CAZyme ID: MGYG000000014_04138
• CAZy Family: GH23
• CAZyme Description: Membrane-bound lytic murein transglycosylase C

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
275		29977.17	4.4399

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000014	4564499	Isolate	United Kingdom	Europe

• Gene Location: Start: 167; End: 994 Strand: -

Full Sequence      

MPIDGLSNNISNEQLMAMSLMSNGQLTNESTSSTESSEYNNLAFQMMMKNYMDSAKNTAK
DNVDKIVNNSNTENNNSTTEVKKQTDASDSINAAAASNQTSRAVQNYLAGQKLTDIPLTL
NNSYGNIYSSGTSMLNNRTPEDLKKIYSAVSDASKKYGISESLILAVIKQESDFDSTCTS
SVGASGLMQIMPGNYSHLGISDPYDVDQNVNGGTKLLREYLDKYNGDIQMALMAYNGGPG
TMQRRGVASSDELYKMPEETQNYVPKVMGYYQSGV

Enzyme Prediction     

No EC number prediction in MGYG000000014_04138.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	160	273	7.6e-29	0.8

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00254	LT-like	2.25e-40	161	272	1	111	lytic transglycosylase(LT)-like domain. Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
cd16896	LT_Slt70-like	1.74e-32	144	272	2	145	uncharacterized lytic transglycosylase subfamily with similarity to Slt70. Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
cd13401	Slt70-like	1.91e-30	148	272	8	147	70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
pfam01464	SLT	2.68e-27	153	244	4	101	Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
cd13403	MLTF-like	4.47e-21	152	244	3	101	membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins. This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK75332.1	5.21e-188	1	275	1	275
QMW92413.1	5.21e-188	1	275	1	275
AXB86212.1	6.07e-187	1	275	1	275
QCJ01583.1	1.43e-185	1	275	1	275
AOR92895.1	1.43e-185	1	275	1	275

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FBT_A	1.28e-10	154	270	457	588	ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A	1.30e-10	154	270	486	617	TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
6FC4_A	3.10e-10	154	270	458	589	ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
6FCQ_A	3.10e-10	154	270	457	588	ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa],6FCR_A Chain A, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa],6FCS_A Chain A, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa],6FCU_A Chain A, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
1QSA_A	3.10e-10	149	270	452	594	CrystalStructure Of The 70 Kda Soluble Lytic Transglycosylase Slt70 From Escherichia Coli At 1.65 Angstroms Resolution [Escherichia coli],1QTE_A Crystal Structure Of The 70 Kda Soluble Lytic Transglycosylase Slt70 From Escherichia Coli At 1.90 A Resolution In Complex With A 1,6- Anhydromurotripeptide [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31608	5.04e-34	146	273	60	181	Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O64046	2.85e-25	145	275	1421	1545	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	2.85e-25	145	275	1421	1545	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P27380	1.61e-17	147	238	8	98	Transglycosylase OS=Enterobacteria phage PRD1 OX=10658 GN=VII PE=1 SV=3
A8GJ50	1.49e-10	127	251	172	312	Membrane-bound lytic murein transglycosylase C OS=Serratia proteamaculans (strain 568) OX=399741 GN=mltC PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000014_04138.