CAZyme Information: MGYG000001388_03779

Basic Information

• Species: Desulfitobacterium hafniense
• Lineage: Bacteria; Firmicutes_B; Desulfitobacteriia; Desulfitobacteriales; Desulfitobacteriaceae; Desulfitobacterium; Desulfitobacterium hafniense
• CAZyme ID: MGYG000001388_03779
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
230		25391.8	6.9189

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001388	5194328	Isolate	not provided	not provided

• Gene Location: Start: 265398; End: 266090 Strand: +

Full Sequence      

MNHEGHERRGFCRKGCALLFMCCFWVNAWSLPAFAQEEERVTYSVVTLQAGQSLDDLAQK
YQTTRSQILLDNPAVVIAPGATLTIREKTVQGTHEAAEVLSRGTALIWSWPAYGSISSDY
GWRKGEFHHGIDLAISHGTEILAARAGKVVKAQWHDIYGLTVLLEHGNGVQSLYAHNQKI
LVSPGEWVEQGDCIALAGDTGRSTGPHLHFEIRLHGKAVDPKPYLPQNPI

Enzyme Prediction     

No EC number prediction in MGYG000001388_03779.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01551	Peptidase_M23	1.04e-45	126	221	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.
COG0739	NlpD	1.25e-44	33	230	54	269	Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
cd12797	M23_peptidase	6.50e-39	128	212	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.
PRK11637	PRK11637	4.88e-28	102	225	304	426	AmiB activator; Provisional
COG4942	EnvC	3.37e-27	109	225	300	418	Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAE86725.1	9.88e-175	1	230	1	230
CDX05095.1	3.31e-173	1	230	1	230
AGA70845.1	1.78e-110	1	226	1	234
AHF08289.1	2.09e-69	30	227	10	214
QAA76629.1	2.17e-41	47	226	95	280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BH5_A	1.71e-25	102	225	18	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	1.68e-23	102	225	262	384	EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
6JMX_A	4.24e-20	84	221	94	242	ChainA, Peptidase M23 [Campylobacter jejuni],6JMY_A Chain A, Peptidase M23 [Campylobacter jejuni],6KV1_A Chain A, Peptidase M23 [Campylobacter jejuni]
2HSI_A	1.11e-19	111	221	157	273	Crystalstructure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1],2HSI_B Crystal structure of putative peptidase M23 from pseudomonas aeruginosa, New York Structural Genomics Consortium [Pseudomonas aeruginosa PAO1]
6JN1_A	9.99e-19	84	221	94	242	ChainA, Peptidase M23 [Campylobacter jejuni]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37690	1.23e-22	102	225	295	417	Murein hydrolase activator EnvC OS=Escherichia coli (strain K12) OX=83333 GN=envC PE=1 SV=2
Q8K9M4	4.27e-22	128	221	291	384	Uncharacterized metalloprotease BUsg_310 OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=BUsg_310 PE=3 SV=1
P0AFT0	2.47e-21	128	221	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mepM PE=3 SV=1
P0AFS9	2.47e-21	128	221	314	407	Murein DD-endopeptidase MepM OS=Escherichia coli (strain K12) OX=83333 GN=mepM PE=1 SV=1
P0AFT1	2.47e-21	128	221	314	407	Murein DD-endopeptidase MepM OS=Shigella flexneri OX=623 GN=mepM PE=3 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
0.012623	0.939379	0.046714	0.000640	0.000317	0.000280

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001388_03779.