CAZyme Information: MGYG000001261_00255

Basic Information

• Species: Caulobacter sp903900155
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Caulobacter; Caulobacter sp903900155
• CAZyme ID: MGYG000001261_00255
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
384	MGYG000001261_8|CGC1	41687.53	8.7006

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001261	5012197	MAG	Italy	Europe

• Gene Location: Start: 15614; End: 16768 Strand: +

Full Sequence      

MTNELFRRLTTVYLGEAIRYPKLRAVTLAQWALESGRGGSVLARDHYNFGGLKWRKEMTP
YATKVKYAAHDGEDFYCKFATLENFIAGYWAFLNRTPYSGWEANVATPEKFIRFIGPTYA
PRPDYADAVLALVPEAEALLADVEKAEVAAVKPAVVPASLGAIVIDPGHGGTSDVSGSSA
NNAISASNVKEKKLTLDFALILRDELLRQAAARNETVQVVLTRTTDVNVTGKARAAMAFD
HKAKLFLCIHFNGAKTATIRGAETFYRAKENDNINLEADMEFAGAVQKALFTALKTLDPG
AKDRGVKPDNQGNPNLPGFGVLNDISLGNDRRQTPCRAAYIEAEFITNPSVDKLLISGPN
AVQNRTAAMAAVAGACLTQMRNIP

Enzyme Prediction     

No EC number prediction in MGYG000001261_00255.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	24	132	5.7e-17	0.828125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	9.30e-38	163	357	2	156	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.
pfam01520	Amidase_3	5.51e-34	163	357	1	157	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG0860	AmiC	5.81e-27	163	357	45	209	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
TIGR02883	spore_cwlD	6.93e-16	163	355	3	169	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]
pfam01832	Glucosaminidase	8.02e-11	16	91	7	79	Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIJ44785.1	9.63e-172	3	383	4	388
AHE53903.1	1.04e-150	4	384	5	383
AHZ45666.1	3.10e-147	3	384	4	382
BAC89304.1	8.78e-119	3	381	26	398
AGY58716.1	5.46e-105	3	377	2	380

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4RN7_A	4.88e-14	163	357	6	163	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5J72_A	1.55e-08	163	354	454	616	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	6.69e-07	163	360	7	171	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	1.32e-06	163	252	4	81	N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001261_00255.