CAZyme Information: MGYG000001450_02029

Basic Information

• Species: Nesterenkonia massiliensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Nesterenkonia; Nesterenkonia massiliensis
• CAZyme ID: MGYG000001450_02029
• CAZy Family: GH23
• CAZyme Description: Membrane-bound lytic murein transglycosylase F

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
306	MGYG000001450_6|CGC1	32340.93	4.1782

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001450	2641047	Isolate	not provided	Europe

• Gene Location: Start: 64520; End: 65440 Strand: -

Full Sequence      

MPDEYWEAIEAAAAHSGISTDVLAAQIQQESGWNPNAQSPAGAQGIAQFMPGTAAQYGLD
PFDPIASIEAQGRYMADLQEEVGSLASNERELIELTLAAYNAGPGAVQQHGGIPPFAETQ
HYVETILESAQGNFSANCAPPGGFYADVRDLGPGEWTHPLPGGIVTSRFGPRPCPIANAL
NCHNGVSDHRGIDIATPPPGSTIVAPMELEIRAVGTQPGLGETVLAIMTEEPYLHVEFGH
CRYNSFYVSAGDIVPPGTPLCHEGTTGNSAAIHLHLQFGTPDGAWDQAGWDNLIDPEPFL
RAKGIL

Enzyme Prediction     

No EC number prediction in MGYG000001450_02029.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	19	137	3.3e-32	0.837037037037037

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00254	LT-like	1.45e-36	23	131	4	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.
cd13403	MLTF-like	2.37e-29	9	109	1	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.
cd13401	Slt70-like	1.06e-28	5	131	6	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.
cd13399	Slt35-like	1.77e-28	16	131	1	107	Slt35-like lytic transglycosylase. Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) 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 to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
pfam01464	SLT	1.37e-25	9	122	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
CBT77213.1	3.18e-89	1	305	63	373
ALQ32542.1	4.78e-89	1	305	65	375
QRQ80560.1	1.27e-88	1	305	63	373
BBE24542.1	1.05e-74	1	304	74	378
AOY74432.1	2.44e-70	1	306	51	359

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QSA_A	3.50e-08	28	127	476	592	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	6.18e-07	28	127	476	592	ComplexOf The 70-Kda Soluble Lytic Transglycosylase With Bulgecin A [Escherichia coli]
5MPQ_A	4.46e-06	27	130	438	552	BulgecinA: The key to a broad-spectrum inhibitor that targets lytic transglycosylases [Neisseria meningitidis]
5O1J_A	4.47e-06	27	130	442	556	Lytictransglycosylase in action [Neisseria meningitidis MC58]
6FPN_B	4.48e-06	27	130	448	562	Lytictransglycosylase in action [Neisseria meningitidis MC58]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O64046	2.48e-30	4	304	1421	1682	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1
O31976	2.48e-30	4	304	1421	1682	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
O31608	1.06e-21	8	126	63	175	Putative murein lytic transglycosylase YjbJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yjbJ PE=3 SV=1
Q0A9T8	2.15e-08	5	105	283	383	Membrane-bound lytic murein transglycosylase F 2 OS=Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) OX=187272 GN=mltF2 PE=3 SV=1
P0AGC4	1.95e-07	28	127	503	619	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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001450_02029.