CAZyme Information: MGYG000002341_02690

Basic Information

• Species: Acinetobacter ursingii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter ursingii
• CAZyme ID: MGYG000002341_02690
• CAZy Family: GH23
• CAZyme Description: Membrane-bound lytic murein transglycosylase F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
285	MGYG000002341_19|CGC1	31162.77	10.0723

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002341	3456217	Isolate	United States	North America

• Gene Location: Start: 24692; End: 25549 Strand: -

Full Sequence      

MKKSVHFSLHFILGAVVTAIMTVATHAGQIYIYKDREGGTLLTNRKSSDRSLTKIKATYY
PDSNIHSYRNWGNSEAAVLPSYSKNKNAFDQIIRQAAQQHGISEGLIKAVMHTESGFNTN
ARSPVGAQGLMQLMPATAKRFNVSNVYDPYENIFGGAKYLSWLLKRFNGNTQLALAAYNA
GEGNVDKYGGIPPFRETQDYVHRVTSRFNNLYASGVSNSSTTTPAPQIIAQSANYSSATA
ANPRTDNPTKYSRQVISVSNNSFTDAPGTYVTDNATASARIHISN

Enzyme Prediction     

No EC number prediction in MGYG000002341_02690.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	106	213	4.2e-33	0.8

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00254	LT-like	1.07e-51	104	209	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.
cd13401	Slt70-like	7.03e-46	88	206	5	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	6.42e-43	91	204	6	140	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	3.70e-40	93	211	1	159	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	1.51e-36	93	200	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
QQT67215.1	3.19e-203	1	285	1	285
QQT85290.1	3.19e-203	1	285	1	285
BBF78150.1	9.14e-203	1	285	1	285
CAG69563.1	3.43e-147	1	285	1	283
QTD63773.1	2.35e-136	1	284	1	294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FBT_A	1.06e-15	92	206	453	587	ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A	1.09e-15	92	206	482	616	TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
6FCQ_A	2.60e-15	92	206	453	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	2.60e-15	92	206	454	588	ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
1QSA_A	2.25e-13	88	204	452	591	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	7.48e-43	60	206	21	177	Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O64046	1.12e-40	72	218	1408	1551	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	1.12e-40	72	218	1408	1551	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P27380	3.65e-17	91	214	9	125	Transglycosylase OS=Enterobacteria phage PRD1 OX=10658 GN=VII PE=1 SV=3
Q3IHZ1	3.21e-13	106	186	296	382	Membrane-bound lytic murein transglycosylase F OS=Pseudoalteromonas translucida (strain TAC 125) OX=326442 GN=mltF PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.013125	0.984982	0.000977	0.000338	0.000255	0.000271

TMHMM  Annotations     

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