CAZyme Information: MGYG000000690_00774

Basic Information

• Species: CAG-590 sp000431135
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-590; CAG-590 sp000431135
• CAZyme ID: MGYG000000690_00774
• CAZy Family: GH23
• CAZyme Description: Membrane-bound lytic murein transglycosylase F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
230	MGYG000000690_11|CGC1	24467.08	4.2928

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000690	2764780	MAG	Kazakhstan	Asia

• Gene Location: Start: 47392; End: 48084 Strand: +

Full Sequence      

MQTIRSIDQNDPYTYRNKQSNTPASSSDFDQIFQNETIIYADAADDTTFMNPQGVVVSKP
TEAVITGTSFSDSSSNITAPGDLDPIFEQAANQYGVRKDLLIAVARAESNFNASVVSGAG
AIGIMQLMPETARNLGVKDPYNATDNIMGGAKYLSRLLSQYNGNISLALAAYNAGSGNVE
KYGGIPPFKETQTYVRKILADIGETENSVASDPAAVTIYAVAANSATHTL

Enzyme Prediction     

No EC number prediction in MGYG000000690_00774.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	98	206	1.9e-32	0.8074074074074075

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00254	LT-like	8.98e-48	99	200	2	108	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.
cd13401	Slt70-like	1.73e-43	85	200	8	144	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.
cd16896	LT_Slt70-like	1.75e-42	88	201	9	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.
cd13403	MLTF-like	1.05e-35	87	186	1	113	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.
pfam01464	SLT	4.94e-34	87	194	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEN96200.1	5.85e-54	74	217	56	199
CBL07423.1	2.10e-52	34	216	30	217
CBL11165.1	2.97e-52	34	216	30	217
VCV21029.1	2.97e-52	34	216	30	217
QUO22855.1	2.42e-50	57	207	25	181

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FBT_A	1.33e-14	91	200	457	587	ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A	1.35e-14	91	200	486	616	TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
6FCQ_A	3.30e-14	91	200	457	587	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]
6FC4_A	3.30e-14	91	200	458	588	ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
1QSA_A	1.51e-10	86	200	456	593	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	1.24e-44	58	198	33	175	Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O31976	1.98e-37	64	211	1400	1550	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
O64046	1.98e-37	64	211	1400	1550	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
P27380	1.63e-15	90	202	14	119	Transglycosylase OS=Enterobacteria phage PRD1 OX=10658 GN=VII PE=1 SV=3
Q0A9W6	1.02e-12	87	180	296	395	Membrane-bound lytic murein transglycosylase F 1 OS=Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) OX=187272 GN=mltF1 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
1.000013	0.000023	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000690_00774.