CAZyme Information: MGYG000002501_00008

Basic Information

• Species: Enterobacter cloacae_K
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter cloacae_K
• CAZyme ID: MGYG000002501_00008
• CAZy Family: CBM50
• CAZyme Description: Murein hydrolase activator NlpD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
247		26118.8	10.3301

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002501	4737021	Isolate	France	Europe

• Gene Location: Start: 6296; End: 7039 Strand: -

Full Sequence      

MFAGSLTRNPITAIFCLTLTLLLVGCSGSKSSDTGSYSGSVYTVKRGDTLYRISRATGTS
VKDLARLNNLSPPYTIEVGQQLKVSGGSSSGKKSSSKGKTAKVTPSYQVPQSSWPPVGQR
CWIWPASGKVVAPYSLSEGGNKGIDIAAARGTPVYASGAGKVVYVGNQLRGYGNLIMIKH
GEDYITAYAHNDTMLVNNGQNVKAGQKIATMGSTGTDSVKLHFQIRYKATAIDPQRYLPA
PGSKPKC

Enzyme Prediction     

No EC number prediction in MGYG000002501_00008.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10871	nlpD	5.04e-76	16	239	16	317	murein hydrolase activator NlpD.
COG0739	NlpD	3.00e-51	39	247	1	273	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551	Peptidase_M23	2.56e-42	139	234	1	96	Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
COG4942	EnvC	1.93e-33	115	238	294	418	Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].
cd12797	M23_peptidase	3.88e-33	141	225	1	85	M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAZ64234.1	1.34e-176	1	247	1	247
BBJ68959.1	1.34e-176	1	247	1	247
QBN11750.1	1.34e-176	1	247	1	247
AZV07069.1	1.34e-176	1	247	1	247
QLC84238.1	5.44e-176	1	247	1	247

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BH5_A	5.95e-16	116	238	17	140	LytMdomain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_B LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_C LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_D LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12]
6TPI_A	1.36e-14	116	238	261	384	EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
2GU1_A	1.62e-12	125	236	224	327	Crystalstructure of a zinc containing peptidase from vibrio cholerae [Vibrio cholerae]
6UE4_A	4.50e-12	129	246	261	372	ShyAEndopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961],6UE4_B ShyA Endopeptidase from Vibrio cholerae (Closed form) [Vibrio cholerae O1 biovar El Tor str. N16961]
6U2A_A	4.53e-12	129	246	258	369	ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q46798	1.17e-133	1	247	1	251	Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P0ADA4	5.40e-60	35	239	116	377	Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1
P0ADA3	5.40e-60	35	239	116	377	Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
Q56131	4.04e-58	35	239	109	371	Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P39700	4.48e-58	35	239	113	375	Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000005	1.000037	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002501_00008.