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CAZyme Information: MGYG000004821_00060

You are here: Home > Sequence: MGYG000004821_00060

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 Limosilactobacillus timonensis
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus timonensis
CAZyme ID MGYG000004821_00060
CAZy Family GH23
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
693 77103.36 4.9307
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004821 1280697 MAG China Asia
Gene Location Start: 10570;  End: 12651  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004821_00060.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd13402 LT_TF-like 1.14e-33 259 348 1 89
lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
pfam18994 Prophage_tailD1 2.03e-19 11 91 5 84
Prophage endopeptidase tail N-terminal domain. This domain represents the N-terminal domain of prophage tail proteins that are probably acting as endopeptidases. This domain has a RIFT related fold.
pfam06605 Prophage_tail 3.61e-17 94 238 5 133
Prophage endopeptidase tail. This family is of prophage tail proteins that are probably acting as endopeptidases.
cd12797 M23_peptidase 8.01e-15 391 476 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.
pfam01551 Peptidase_M23 1.27e-13 389 482 1 93
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AMS08292.1 0.0 1 693 1 693
QAR23048.1 0.0 1 693 1 693
ADW01240.1 0.0 1 693 1 693
SNX31922.1 0.0 1 693 1 693
QAR23002.1 0.0 1 656 1 656

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GT1_A 8.09e-48 361 508 25 173
ChainA, Choline binding protein A [Ligilactobacillus salivarius str. Ren]
3GS9_A 3.14e-14 28 214 26 214
Crystalstructure of prophage tail protein gp18 (NP_465809.1) from Listeria monocytogenes EGD-e at 1.70 A resolution [Listeria monocytogenes EGD-e]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000048 0.000006 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004821_00060.