CAZyme Information: MGYG000001469_02709

Basic Information

• Species: Neobacillus jeddahensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-18226; Neobacillus; Neobacillus jeddahensis
• CAZyme ID: MGYG000001469_02709
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
480	MGYG000001469_28|CGC1	51666.37	7.0397

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001469	4762944	Isolate	not provided	not provided

• Gene Location: Start: 15073; End: 16515 Strand: -

Full Sequence      

MKLYVDPGHGGTDPGAQGNGLNEKDLTLDIALKLQSILTNGYENIEIKLSRTSDVTKSLS
QRTNEANSWGANYYLAIHINAANGSAQGYEDYIYSGLSNTSPTANYQTIIHAEVMKLNQL
TDRGRKKANFHVLRESTMPAFLSENGFIDNAHDTALMKQASWRQNVAQGHANGLAKAFNL
KAKATPPPAPSDPGAGALYRVIAGSFQTRENADERVTFLRSKGIDSFVNTTTLSGKTWFR
VQAGAYSNRENAEKRLAEVKKAGIGDAFLVVENGGATPAESSSGNDNSTGGNNDNSGSGN
SSDMTIGSNSIMGPTSLSGAQMNAYVKTINPNAPDLGNFYQNLGEYYGIRGDIAFAQAIH
ETNYFRFTGTVKTEQNNYAGIGATGGSQTGANFATPQEGVLAHLQHLYAYATTTPLPPQY
PLVDPRFSLVTRGSAPRWIDLNGKWAVPGETYGQMILELYAKIVSHTIKNLQTILTELPS

Enzyme Prediction     

No EC number prediction in MGYG000001469_02709.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	7.76e-59	5	175	4	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	8.68e-55	1	181	43	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520	Amidase_3	8.68e-51	4	174	2	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	8.46e-32	63	174	1	113	Ami_3 domain.
TIGR02883	spore_cwlD	1.83e-23	3	174	3	186	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
QCJ41002.1	2.87e-204	1	479	1	462
QCJ44336.1	7.04e-199	1	474	1	453
QGQ48088.1	1.16e-196	1	477	1	450
AWG44825.1	6.47e-185	1	478	1	445
QOK28651.1	1.85e-184	1	477	1	453

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	2.39e-25	1	181	1	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	7.96e-19	3	181	6	185	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	2.29e-18	1	176	5	176	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
5J72_A	2.03e-14	3	153	454	612	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]
3NE8_A	2.04e-11	1	187	5	233	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37134	1.36e-73	1	228	2	214	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
Q06320	4.98e-71	1	228	2	215	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
O48471	1.09e-40	3	235	5	247	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
P54525	6.88e-21	3	174	32	200	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q02114	1.11e-20	3	173	322	490	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 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
1.000069	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001469_02709.