CAZyme Information: MGYG000000147_01656

Basic Information

• Species: Bacillus paralicheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis
• CAZyme ID: MGYG000000147_01656
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase CwlA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
330	MGYG000000147_2|CGC19	35213.16	10.459

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000147	4371304	Isolate	United Kingdom	Europe

• Gene Location: Start: 737338; End: 738330 Strand: +

Full Sequence      

MAISVRKNLVASSKHSLKCPYSMNAKYITFHNTANDASAANEIAYMIRNNNQVSYHFAVD
DKEVVQGIPTNRNAWHCGDGNGPGNRSSIGVEVCYSKSGGAKYKAAEKLAIKFIAQLLKE
RGWGVDRVKKHQDWSGKYCPHRVLDEGRWDAVKAAIAAELKALGGKSSSSASKPSGSTYT
VKKGDTLSAIAKANGVSVASLQSWNNIKDPNKIYVGQVLKLKGTPKPAAAPKPSGSSKKT
FTLPGGVLKVTSPLTKGTKVTQVQDALAAVYFYPDKGAKNNGIDGYYGPKTANAVKRFQS
MHGLSQDGIYGPNTKAKLAAALKKAGYSVN

Enzyme Prediction     

No EC number prediction in MGYG000000147_01656.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG5632	CwlA	8.27e-59	3	161	2	170	N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis].
cd06583	PGRP	6.47e-30	24	142	1	125	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.
smart00644	Ami_2	7.41e-29	23	140	1	126	Ami_2 domain.
pfam01510	Amidase_2	2.17e-27	26	142	3	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	2.94e-17	178	221	2	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
QSV41397.1	1.49e-226	1	330	1	330
QBJ82979.1	4.94e-166	1	323	1	324
QHL55113.1	4.94e-166	1	323	1	324
ADM37946.1	1.62e-162	1	323	1	325
QDD03075.1	1.62e-162	1	323	1	325

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YB0_A	9.69e-64	3	151	1	149	Structureof PlyL [Bacillus anthracis],1YB0_B Structure of PlyL [Bacillus anthracis],1YB0_C Structure of PlyL [Bacillus anthracis]
2AR3_A	8.03e-63	3	151	1	149	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]
2L47_A	5.35e-62	3	151	1	149	Solutionstructure of the PlyG catalytic domain [Bacillus phage Gamma]
3HMB_A	4.04e-32	21	156	22	156	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]
3RDR_A	8.93e-30	21	156	22	156	Structureof the catalytic domain of XlyA [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34391	6.12e-145	1	322	1	317	N-acetylmuramoyl-L-alanine amidase XlyB OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyB PE=3 SV=1
P24808	1.02e-125	1	323	1	272	N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlA PE=1 SV=1
P39800	6.40e-80	21	322	19	296	N-acetylmuramoyl-L-alanine amidase XlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyA PE=1 SV=1
P54450	1.17e-53	3	323	2	250	N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1
P36550	2.54e-51	3	323	2	360	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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000147_01656.