CAZyme Information: MGYG000000012_00501

Basic Information

• Species: Bacillus subtilis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis
• CAZyme ID: MGYG000000012_00501
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase XlyA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
297	MGYG000000012_1|CGC5	31917.72	5.2757

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000012	4053580	Isolate	United Kingdom	Europe

• Gene Location: Start: 455383; End: 456276 Strand: +

Full Sequence      

MVNIIQDFIPVGANNRPGYAMTPLYITVHNTANTAVGADAAAHARYLKNPDTTTSWHFTV
DDTEIYQHLPLNENGWHAGDGNGSGNRASIGIEICENADGDFAKATANAQWLIKTLMAEH
NISLANVVPHKYWSGKECPRKLLDTWDSFKAGIGGGGSRTYVVKQGDTLTSIAKAFSVTV
AQLQEWNNIEDPNLIQVGQVLIVSAPSSAEEPELYPLPDGIIQLTTPYTSGEHVFQVQRA
LAALYFYPDKGAVNNGIDGIYSPKTADAVARFQSVNGLTADGIYGPATKAKIAAQLS

Enzyme Prediction     

No EC number prediction in MGYG000000012_00501.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG5632	CwlA	9.71e-58	1	160	1	172	N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis].
smart00644	Ami_2	1.33e-28	21	139	1	126	Ami_2 domain.
cd06583	PGRP	2.19e-28	23	140	2	124	Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.
pfam01510	Amidase_2	7.76e-27	22	141	1	121	N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.
cd00118	LysM	1.14e-16	159	203	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASB60559.1	2.77e-219	1	297	1	297
AUS13516.1	2.77e-219	1	297	1	297
QRZ94275.1	3.78e-217	1	297	1	297
AEP90410.1	1.54e-216	1	297	1	297
API95326.1	1.42e-212	1	297	1	297

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3RDR_A	1.33e-114	1	154	4	157	Structureof the catalytic domain of XlyA [Bacillus subtilis]
3HMB_A	6.92e-110	1	154	4	157	ChainA, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_B Chain B, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_C Chain C, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis]
2L47_A	2.13e-29	19	160	19	161	Solutionstructure of the PlyG catalytic domain [Bacillus phage Gamma]
1YB0_A	5.33e-28	9	149	9	150	Structureof PlyL [Bacillus anthracis],1YB0_B Structure of PlyL [Bacillus anthracis],1YB0_C Structure of PlyL [Bacillus anthracis]
2AR3_A	4.15e-27	9	149	9	150	ChainA, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_B Chain B, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_C Chain C, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39800	8.71e-208	1	297	1	297	N-acetylmuramoyl-L-alanine amidase XlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyA PE=1 SV=1
P54450	7.57e-112	1	296	1	249	N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1
O34391	4.54e-76	20	296	22	317	N-acetylmuramoyl-L-alanine amidase XlyB OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyB PE=3 SV=1
P24808	3.29e-56	25	296	27	271	N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlA PE=1 SV=1
P36550	3.55e-36	1	292	1	355	N-acetylmuramoyl-L-alanine amidase CwlL OS=Bacillus licheniformis OX=1402 GN=cwlL 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
0.999721	0.000281	0.000026	0.000001	0.000001	0.000007

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000012_00501.