CAZyme Information: MGYG000001712_03487

Basic Information

• Species: Bacillus_A thuringiensis_S
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A thuringiensis_S
• CAZyme ID: MGYG000001712_03487
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410	MGYG000001712_1|CGC29	45471.15	8.8199

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001712	5736823	Isolate	United States	North America

• Gene Location: Start: 3450664; End: 3451896 Strand: -

Full Sequence      

MKYKLIATGILAGSLLTYSSNTFANTHKFPDVPAWADKSVNYLVDKQVLNGYPDGTFGSN
DSLDRASATKIMTKVLGIQIDSNAKPSFTDSQNHWATPYIAAAEKAGIVKGEGNGIFNPS
GKVTRAAMATMLVNAYKLQSAANHNEQVKFEDLKGHWGEKYANILIGLKISNGTENGWQP
NRFITRAEAAQLTAKTDMMQHRPQNPLESKTIIIDPGHGGEDPGKSTKGLPESKIVLDTS
LRLQQLLEKHTPFTVLLTRQSDNRPGHDQKSSLQERVKFAKKNQGDIFISVHANAFNGNA
KGTETYYYKSSKSEKTNPHVEESRVLAEKIQTRLVEALQTRDRGVKHGDLHVIRENDMPA
VLTELAFIDNGIDYSKLSTEDGRQIAAEAIYEGILDYYEWKGNNVSEYRL

Enzyme Prediction     

No EC number prediction in MGYG000001712_03487.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	4.21e-67	211	395	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	2.56e-60	181	401	24	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520	Amidase_3	1.06e-57	212	394	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.
TIGR02883	spore_cwlD	3.82e-40	210	397	1	189	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]
smart00646	Ami_3	1.13e-34	277	394	1	113	Ami_3 domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCY61611.1	1.58e-130	1	213	1	210
ANP81487.1	1.58e-130	1	213	1	210
AMR05776.1	4.48e-130	1	213	1	210
AYF85542.1	4.48e-130	1	213	1	210
ANC11239.1	6.35e-130	1	213	1	210

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6BT4_A	5.29e-52	29	197	26	196	Crystalstructure of the SLH domain of Sap from Bacillus anthracis in complex with a pyruvylated SCWP unit [Bacillus anthracis]
3PYW_A	5.46e-52	29	197	5	175	Thestructure of the SLH domain from B. anthracis surface array protein at 1.8A [Bacillus anthracis]
1JWQ_A	1.20e-25	210	401	2	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	4.00e-25	211	403	5	187	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5J72_A	6.22e-22	210	396	452	635	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9RMZ0	1.32e-144	6	408	10	530	Uncharacterized cell wall amidase pXO2-42/BXB0045/GBAA_pXO2_0045 OS=Bacillus anthracis OX=1392 GN=pXO2-42 PE=3 SV=2
P49052	2.76e-58	3	205	7	212	S-layer protein OS=Bacillus licheniformis OX=1402 PE=3 SV=1
P94217	4.10e-56	3	205	7	212	S-layer protein EA1 OS=Bacillus anthracis OX=1392 GN=eag PE=3 SV=1
P49051	9.44e-48	3	213	7	220	S-layer protein sap OS=Bacillus anthracis OX=1392 GN=sap PE=1 SV=1
Q9ZES5	4.06e-46	3	197	7	205	S-layer protein OS=Bacillus thuringiensis subsp. finitimus OX=29337 GN=ctc PE=1 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
0.000301	0.999002	0.000206	0.000176	0.000170	0.000153

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001712_03487.