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CAZyme Information: MGYG000002868_01466

You are here: Home > Sequence: MGYG000002868_01466

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 CAG-279 sp900556245
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-279; CAG-279 sp900556245
CAZyme ID MGYG000002868_01466
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
399 44613.62 9.6611
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002868 1593426 MAG United States North America
Gene Location Start: 1030;  End: 2229  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002868_01466.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10783 mltD 1.95e-36 18 345 171 455
membrane-bound lytic murein transglycosylase D; Provisional
cd16894 MltD-like 2.46e-24 15 87 58 129
Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
PRK06347 PRK06347 3.78e-21 184 398 385 591
1,4-beta-N-acetylmuramoylhydrolase.
PRK06347 PRK06347 2.11e-18 169 396 292 521
1,4-beta-N-acetylmuramoylhydrolase.
pfam01476 LysM 1.33e-14 297 339 1 43
LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQR10036.1 1.08e-121 15 399 186 546
ANU62627.1 1.08e-121 15 399 186 546
BCI63615.1 3.58e-109 15 398 188 576
AHF12926.1 1.47e-96 15 338 143 442
QCD38174.1 5.07e-95 18 399 189 570

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2MKX_A 2.55e-10 296 341 6 51
Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P37710 9.11e-24 184 398 345 540
Autolysin OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0799 PE=1 SV=2
P0AEZ7 4.55e-22 18 339 169 445
Membrane-bound lytic murein transglycosylase D OS=Escherichia coli (strain K12) OX=83333 GN=mltD PE=1 SV=1
P0AEZ8 4.55e-22 18 339 169 445
Membrane-bound lytic murein transglycosylase D OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=mltD PE=3 SV=1
P54421 1.54e-15 207 398 29 192
Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE PE=1 SV=1
Q49UX4 4.51e-12 297 398 29 129
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1

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
0.982423 0.016567 0.000710 0.000061 0.000028 0.000210

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002868_01466.