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CAZyme Information: MGYG000002458_03678

You are here: Home > Sequence: MGYG000002458_03678

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Yersinia aleksiciae
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia aleksiciae
CAZyme ID MGYG000002458_03678
CAZy Family CBM50
CAZyme Description Murein hydrolase activator NlpD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
321 33669.44 9.3148
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002458 4525402 Isolate Finland Europe
Gene Location Start: 40601;  End: 41566  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002458_03678.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10871 nlpD 0.0 1 321 7 319
murein hydrolase activator NlpD.
COG0739 NlpD 1.09e-54 72 319 3 265
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 2.40e-41 219 314 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 9.15e-34 176 318 273 418
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].
cd12797 M23_peptidase 1.82e-29 221 305 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AKP34390.1 1.28e-227 1 321 1 321
QKJ09031.1 1.74e-225 1 321 1 321
QKJ05289.1 1.43e-224 1 321 1 321
QDW34608.1 1.79e-224 1 321 7 327
QKJ17776.1 3.77e-220 1 321 1 321

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BH5_A 2.46e-17 196 318 15 140
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 8.40e-16 196 318 259 384
EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
2B44_A 7.46e-12 204 321 8 133
TruncatedS. aureus LytM, P 32 2 1 crystal form [Staphylococcus aureus],2B44_B Truncated S. aureus LytM, P 32 2 1 crystal form [Staphylococcus aureus]
2B0P_A 7.63e-12 204 321 9 134
truncatedS. aureus LytM, P212121 crystal form [Staphylococcus aureus],2B0P_B truncated S. aureus LytM, P212121 crystal form [Staphylococcus aureus],2B13_A Truncated S. aureus LytM, P41 crystal form [Staphylococcus aureus],2B13_B Truncated S. aureus LytM, P41 crystal form [Staphylococcus aureus],4ZYB_A Chain A, Glycyl-glycine endopeptidase LytM [Staphylococcus aureus subsp. aureus NCTC 8325],4ZYB_B Chain B, Glycyl-glycine endopeptidase LytM [Staphylococcus aureus subsp. aureus NCTC 8325],4ZYB_C Chain C, Glycyl-glycine endopeptidase LytM [Staphylococcus aureus subsp. aureus NCTC 8325],4ZYB_D Chain D, Glycyl-glycine endopeptidase LytM [Staphylococcus aureus subsp. aureus NCTC 8325]
5J1L_A 9.94e-12 223 317 67 163
Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0ADA3 2.59e-132 3 321 9 379
Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4 2.59e-132 3 321 9 379
Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1
Q56131 8.55e-132 3 321 9 373
Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827 3.96e-131 3 321 9 377
Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
P39700 3.96e-131 3 321 9 377
Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000001 1.000036 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002458_03678.