CAZyme Information: MGYG000000502_00125

Basic Information

• Species: Brachyspira aalborgi
• Lineage: Bacteria; Spirochaetota; Brachyspirae; Brachyspirales; Brachyspiraceae; Brachyspira; Brachyspira aalborgi
• CAZyme ID: MGYG000000502_00125
• CAZy Family: GH23
• CAZyme Description: Membrane-bound lytic murein transglycosylase C

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
238	MGYG000000502_1|CGC2	26751.42	6.014

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000502	2577668	MAG	Fiji	Oceania

• Gene Location: Start: 128069; End: 128785 Strand: +

Full Sequence      

MIESIQKIHSRIGEIQNTFNKWGFAPLNTQLPIKPFSEYLNEAMANSSENKINNSDGSLL
IENNIKNNKIDNGKIIDEEAFNGKLSFGVYDDITNNFAKAINAYKKTSTDFPNTYDNIIK
EASEKYSVPEYLIKAVIKQESNYMPNAISSKGAIGLMQIMPSTGALLGVDDKELLKDPYI
NIMTGTKYLSQMLNRYDGRLDLSLSAYNAGPNLVDKLQRIPNIDETKNYVKNIIGYIK

Enzyme Prediction     

No EC number prediction in MGYG000000502_00125.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	121	237	5.4e-29	0.837037037037037

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd13401	Slt70-like	1.72e-46	111	237	2	146	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.
cd00254	LT-like	1.00e-45	132	238	3	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	1.94e-43	115	236	4	143	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.
pfam01464	SLT	8.27e-33	119	229	1	114	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	7.06e-31	119	236	1	155	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
AEM21728.1	8.83e-121	1	238	1	241
AUJ48901.1	4.43e-120	1	238	1	237
QTM02498.1	8.92e-120	1	238	1	237
QTM05061.1	8.92e-120	1	238	1	237
ACN83158.1	8.92e-120	1	238	1	237

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QSA_A	8.67e-15	111	236	449	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]
1SLY_A	1.31e-13	111	236	449	594	ComplexOf The 70-Kda Soluble Lytic Transglycosylase With Bulgecin A [Escherichia coli]
6FBT_A	5.86e-13	111	236	445	588	ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A	5.96e-13	111	236	474	617	TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
6FCQ_A	1.44e-12	111	236	445	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31608	1.80e-34	116	233	61	175	Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O64046	8.90e-27	107	235	1414	1539	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	8.90e-27	107	235	1414	1539	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P0AGC3	4.82e-14	111	236	476	621	Soluble lytic murein transglycosylase OS=Escherichia coli (strain K12) OX=83333 GN=slt PE=1 SV=1
P0AGC4	4.82e-14	111	236	476	621	Soluble lytic murein transglycosylase OS=Escherichia coli O157:H7 OX=83334 GN=slt 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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000502_00125.