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CAZyme Information: MGYG000002526_03686

You are here: Home > Sequence: MGYG000002526_03686

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 Aeromonas hydrophila
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas hydrophila
CAZyme ID MGYG000002526_03686
CAZy Family CBM50
CAZyme Description Murein hydrolase activator NlpD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
346 36731.45 10.2083
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002526 5049466 Isolate United States North America
Gene Location Start: 4048794;  End: 4049834  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002526_03686.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10871 nlpD 6.17e-80 1 346 3 319
murein hydrolase activator NlpD.
COG0739 NlpD 1.05e-45 114 346 2 267
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 2.48e-36 244 339 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.
cd12797 M23_peptidase 1.25e-28 246 330 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.
COG4942 EnvC 1.23e-27 229 339 301 414
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANT69187.1 1.66e-247 1 346 1 346
AHX31350.1 4.57e-245 1 346 1 346
ALQ64903.1 4.57e-245 1 346 1 346
AXV31483.1 4.57e-245 1 346 1 346
AHX68145.1 4.57e-245 1 346 1 346

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6SMK_A 6.44e-08 248 339 31 126
Crystalstructure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_B Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_C Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_D Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583],6SMK_E Crystal structure of catalytic domain A109H mutant of prophage-encoded M23 protein EnpA from Enterococcus faecalis. [Enterococcus faecalis V583]
6UE4_A 3.62e-06 246 340 266 360
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 3.64e-06 246 340 263 357
ShyAendopeptidase from Vibrio cholera (open form) [Vibrio cholerae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q56131 3.35e-61 55 346 114 373
Murein hydrolase activator NlpD OS=Salmonella typhi OX=90370 GN=nlpD PE=3 SV=2
P40827 3.73e-61 55 346 118 377
Murein hydrolase activator NlpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=nlpD PE=3 SV=2
P39700 7.39e-61 55 346 118 377
Murein hydrolase activator NlpD OS=Salmonella dublin OX=98360 GN=nlpD PE=2 SV=2
P0ADA3 7.88e-57 55 346 120 379
Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4 7.88e-57 55 346 120 379
Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1

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 1.000026 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002526_03686.