CAZyme Information: MGYG000004333_00508

Basic Information

• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; UMGS1449
• CAZyme ID: MGYG000004333_00508
• CAZy Family: CBM50
• CAZyme Description: Cell division suppressor protein YneA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
343		38059.01	7.018

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004333	764795	MAG	Israel	Asia

• Gene Location: Start: 26613; End: 27644 Strand: +

Full Sequence      

MNYKIAIDARHGGEDQGYTGNNIIEKDYSLLISNYLKERLDSLGIDNIITRNTDRTLSDD
ARTNIITSAFGNDVKTIVISNGLSNGIGEGLEVIYALRNNDKLASKIAQEVETAGGIVNK
YYQLRDPDDTAKDYYPIIRDTPDYQTIVISYGNVDNSKDAERIKKDYQDYAEAVIKALTS
YIGVKYIPPAGTNYYVVKKGDSLWKIANNYGTSVDELKEENNLKSNILNIGQILLIPKKE
GSASQLQYTVKKGDSLWKIANNNNTTVDALKELNNLKTDTLSIGQILLLPSNSGMNYKIY
IVKKGDSLWKIANSNNITVDALKKLNNLATNLLQIGQSLKIPA

Enzyme Prediction     

No EC number prediction in MGYG000004333_00508.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM50	300	342	5.4e-16	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK06347	PRK06347	3.09e-37	195	343	333	525	1,4-beta-N-acetylmuramoylhydrolase.
PRK06347	PRK06347	5.73e-36	195	341	408	591	1,4-beta-N-acetylmuramoylhydrolase.
cd02696	MurNAc-LAA	1.16e-23	4	179	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	1.28e-19	1	183	41	229	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520	Amidase_3	1.34e-19	5	178	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVK20078.1	1.75e-48	5	342	2	284
QIC05530.1	1.39e-30	5	191	85	265
AYK56267.1	2.52e-30	192	341	173	350
ASV03810.1	2.52e-30	192	341	173	350
QAR78632.1	2.52e-30	192	341	173	350

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J72_A	6.69e-10	5	184	454	631	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]
4B8V_A	1.60e-07	195	342	44	217	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
4UZ2_A	5.23e-06	191	240	1	50	Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O07532	4.67e-30	192	341	173	350	Peptidoglycan endopeptidase LytF OS=Bacillus subtilis (strain 168) OX=224308 GN=lytF PE=1 SV=2
O31852	8.76e-28	189	341	23	200	D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlS PE=1 SV=1
P54421	1.31e-26	163	341	1	192	Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1
P39046	4.54e-20	191	339	485	662	Muramidase-2 OS=Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) OX=768486 GN=EHR_05900 PE=1 SV=1
Q9CIT4	4.32e-18	195	341	243	438	Probable N-acetylmuramidase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=acmA 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
0.999601	0.000373	0.000035	0.000002	0.000001	0.000011

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004333_00508.