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CAZyme Information: MGYG000002399_00439

You are here: Home > Sequence: MGYG000002399_00439

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 hominis
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus hominis
CAZyme ID MGYG000002399_00439
CAZy Family GH23
CAZyme Description putative transglycosylase SceD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
248 26642.73 7.139
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002399 2175331 Isolate not provided not provided
Gene Location Start: 44353;  End: 45099  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002399_00439.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam06737 Transglycosylas 4.04e-23 172 248 1 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 3.79e-19 174 247 1 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 2.80e-05 195 236 51 88
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
QIY36557.1 4.57e-164 1 248 1 248
QDW86423.1 4.57e-164 1 248 1 248
AUW62945.1 4.57e-164 1 248 1 248
AVI06868.1 4.57e-164 1 248 1 248
QKH81843.1 2.27e-148 1 248 1 248

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
Q99SG2 1.07e-77 1 248 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=sceD PE=1 SV=1
A7X4T4 1.07e-77 1 248 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain Mu3 / ATCC 700698) OX=418127 GN=sceD PE=3 SV=1
Q7A4F2 1.07e-77 1 248 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain N315) OX=158879 GN=sceD PE=3 SV=1
Q6GEX9 2.14e-77 1 248 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sceD PE=3 SV=1
Q2FF31 3.04e-77 1 248 1 231
Probable transglycosylase SceD OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sceD PE=3 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
0.000337 0.998868 0.000194 0.000211 0.000192 0.000173

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002399_00439.