CAZyme Information: MGYG000002343_02967

Basic Information

• Species: Acinetobacter courvalinii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter courvalinii
• CAZyme ID: MGYG000002343_02967
• CAZy Family: GH23
• CAZyme Description: Membrane-bound lytic murein transglycosylase F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
289	MGYG000002343_6|CGC1	31620.12	9.8681

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002343	4074146	Isolate	United States	North America

• Gene Location: Start: 40949; End: 41818 Strand: -

Full Sequence      

MNKTTYFFAVCLGTIGFFNATASSYAGQTIYQFKDDNGTTLLTNKKKAEYSHLKVVKATY
YPDSNIHNYSNWGASEASVLPSYSRNKNAFDQLIRQAAQQHGISEGLIKAVMHTESGFNI
KARSPVGAQGLMQLMPATARRFNVSNAYDPQQNIFGGAKYLSWLLKRFNGNTQLAIAAYN
AGEGNVDKYGGIPPFRETQDYVRRVTSRYQNLYASGLGTFTESTSSNTQVLAQSANYSSS
SNNIAEATPAPRSYNRQIITLADGTFTDAPSGTYTTANATATARIRLSN

Enzyme Prediction     

No EC number prediction in MGYG000002343_02967.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	107	214	2.7e-33	0.8

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00254	LT-like	4.49e-53	105	210	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	2.93e-47	89	210	5	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.
cd16896	LT_Slt70-like	4.45e-44	92	210	6	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.
cd13403	MLTF-like	3.63e-38	94	212	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	5.37e-37	94	201	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
QHH94437.1	7.09e-180	1	289	1	292
QHH96035.1	4.85e-179	1	289	2	287
AZM39037.1	2.88e-173	1	289	2	286
AVZ86174.1	2.36e-172	1	289	2	286
ATU46002.1	1.77e-167	1	288	1	285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FBT_A	4.65e-16	93	217	453	596	ChainA, Lytic murein transglycosylase [Pseudomonas aeruginosa]
5OHU_A	4.77e-16	93	217	482	625	TheX-ray Structure of Lytic Transglycosylase Slt from Pseudomonas aeruginosa [Pseudomonas aeruginosa]
6FCQ_A	1.14e-15	93	217	453	596	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	1.14e-15	93	217	454	597	ChainA, Soluble lytic murein transglycosylase [Pseudomonas aeruginosa]
1QSA_A	2.24e-14	89	218	452	603	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	4.77e-45	74	209	35	179	Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
O64046	5.07e-41	73	215	1408	1547	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	5.07e-41	73	215	1408	1547	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
P27380	1.40e-16	92	182	9	98	Transglycosylase OS=Enterobacteria phage PRD1 OX=10658 GN=VII PE=1 SV=3
P39434	3.81e-14	89	218	479	630	Soluble lytic murein transglycosylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=slt PE=3 SV=2

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
0.000902	0.998202	0.000296	0.000187	0.000180	0.000175

TMHMM  Annotations     

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