CAZyme Information: MGYG000000083_00087

Basic Information

• Species: Peribacillus simplex
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-1321; Peribacillus; Peribacillus simplex
• CAZyme ID: MGYG000000083_00087
• CAZy Family: CBM50
• CAZyme Description: Sporulation-specific N-acetylmuramoyl-L-alanine amidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
229		25265.4	7.5078

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000083	5860218	Isolate	United Kingdom	Europe

• Gene Location: Start: 82262; End: 82951 Strand: -

Full Sequence      

MVKVFIDPGHGGTDSGSVGNGLREKDLTLSIATRIKNILLIEYNNVSVKMSRTQDTYPSL
NDRTNAANAWGADFYLSIHINAGGGTGYEDYIYTSSNQITKTYQDHIHSEVMKLINIQDR
GQKTGDLHVLRETDMPALLTENGFIDNVNDAAKLKAASFIESLARGHVNGLVKCFNLTKK
STAVYHTVVNGDTVYSLSIAYGSTVQQIKDWNGLDSQYTITVNQKLRVK

Enzyme Prediction     

No EC number prediction in MGYG000000083_00087.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	1.18e-64	3	172	1	172	N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
COG0860	AmiC	1.87e-64	1	177	42	230	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520	Amidase_3	6.20e-52	4	171	1	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
smart00646	Ami_3	8.63e-36	64	171	1	113	Ami_3 domain.
TIGR02883	spore_cwlD	3.96e-26	4	173	3	188	N-acetylmuramoyl-L-alanine amidase CwlD. Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASS93012.1	7.17e-163	1	229	1	229
QOS88870.1	1.55e-157	1	229	1	229
QYF81207.1	2.21e-157	1	229	1	229
QNK46653.1	5.20e-156	1	229	1	229
AZV60262.1	3.01e-155	1	229	1	229

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RN7_A	4.68e-27	4	172	6	179	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A	5.06e-23	1	173	1	174	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A	8.63e-20	4	173	7	176	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
5J72_A	1.28e-19	4	163	454	625	ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]
4BIN_A	3.42e-16	2	175	174	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37134	6.16e-82	1	202	1	209	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
Q06320	1.24e-79	1	191	1	191	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
O48471	4.34e-46	4	181	5	187	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q02114	2.17e-27	4	175	322	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P54525	7.29e-27	4	171	32	200	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3

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
1.000055	0.000011	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000083_00087.