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CAZyme Information: MGYG000002338_01367

You are here: Home > Sequence: MGYG000002338_01367

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 Staphylococcus haemolyticus
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus haemolyticus
CAZyme ID MGYG000002338_01367
CAZy Family GH23
CAZyme Description putative transglycosylase SceD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
235 24616.03 3.9441
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002338 2548117 Isolate Russia Europe
Gene Location Start: 4251;  End: 4958  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002338_01367.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06737 Transglycosylas 1.18e-20 162 235 4 75
Transglycosylase-like domain. This family of proteins are very likely to act as transglycosylase enzymes related to pfam00062 and pfam01464. These other families are weakly matched by this family, and include the known active site residues.
cd13925 RPF 3.90e-18 166 234 6 70
core lysozyme-like domain of resuscitation-promoting factor proteins. Resuscitation-promoting factor (RPF) proteins, found in various (G+C)-rich Gram-positive bacteria, act to reactivate cultures from stationary phase. This protein shares elements of the structural core of lysozyme and related proteins. Furthermore, it shares a conserved active site glutamate which is required for activity, and has a polysaccharide binding cleft that corresponds to the peptidoglycan binding cleft of lysozyme. Muralytic activity of Rpf in Micrococcus luteus correlates with resuscitation, supporting a mechanism dependent on cleavage of peptidoglycan by RPF.
cd00736 lambda_lys-like 3.55e-04 182 229 51 94
Bacteriophage lambda lysozyme and similar proteins. Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJI70515.1 1.04e-126 1 235 1 235
AMW23878.1 1.04e-126 1 235 1 235
AKC75696.1 1.04e-126 1 235 1 235
BAE04248.1 1.04e-126 1 235 1 235
QFR07441.1 1.04e-126 1 235 1 235

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q4L7X7 2.08e-127 1 235 1 235
Probable transglycosylase SceD OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=sceD PE=3 SV=1
Q5HEA4 1.98e-84 1 235 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain COL) OX=93062 GN=sceD PE=1 SV=1
Q2YUK8 3.99e-84 1 235 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain bovine RF122 / ET3-1) OX=273036 GN=sceD PE=3 SV=1
Q6GEX9 5.66e-84 1 235 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sceD PE=3 SV=1
Q2FWF8 1.14e-83 1 235 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sceD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000579 0.998417 0.000258 0.000265 0.000226 0.000208

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002338_01367.