CAZyme Information: MGYG000002489_00599

Basic Information

• Species: Neisseria gonorrhoeae
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Neisseriaceae; Neisseria; Neisseria gonorrhoeae
• CAZyme ID: MGYG000002489_00599
• CAZy Family: GH23
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
153	MGYG000002489_3|CGC1	17076.9	10.5668

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002489	2153911	Isolate	Canada	North America

• Gene Location: Start: 136227; End: 136688 Strand: -

Full Sequence      

MRLRAILLQFVVPGVLVLTSARAVAFCYKEAGSKYGIDPAMLQSIALTESAFRPNIESHT
ADIGLMGINRSWLPVLHKKFGLTGADVWNPCTNVHIGAWILANSYRQHGKSWEAVGAYNA
ACTKLKGRACYRARMTYANKVYQNWKRLKTRSS

Enzyme Prediction     

No EC number prediction in MGYG000002489_00599.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH23	28	149	4.8e-24	0.8888888888888888

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd13400	LT_IagB-like	3.38e-43	35	147	1	109	Escherichia coli invasion protein IagB and similar proteins. Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. 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. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
PRK15328	PRK15328	1.43e-26	15	153	9	147	type III secretion system invasion protein IagB.
pfam01464	SLT	2.23e-20	29	120	2	94	Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
PRK13722	PRK13722	2.24e-14	27	150	22	147	lytic transglycosylase; Provisional
cd16896	LT_Slt70-like	9.40e-14	33	120	13	104	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZG41891.1	4.89e-110	1	153	1	153
QNV02301.1	4.89e-110	1	153	1	153
SBO64262.1	4.89e-110	1	153	1	153
SBO66516.1	4.89e-110	1	153	1	153
AZG18129.1	4.89e-110	1	153	1	153

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E1WAC2	1.84e-17	25	153	19	147	Invasion protein IagB OS=Salmonella typhimurium (strain SL1344) OX=216597 GN=iagB PE=3 SV=1
P43018	1.84e-17	25	153	19	147	Invasion protein IagB OS=Salmonella typhi OX=90370 GN=iagB PE=3 SV=1
P0CL15	1.84e-17	25	153	19	147	Invasion protein IagB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=iagB PE=3 SV=1
Q8X6H3	1.93e-14	14	148	15	156	Peptidoglycan-binding-like protein OS=Escherichia coli O157:H7 OX=83334 GN=pbl PE=3 SV=1
P14499	3.95e-14	25	143	20	140	X polypeptide OS=Escherichia coli OX=562 GN=X 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
0.008479	0.989840	0.000735	0.000302	0.000297	0.000316

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002489_00599.