Species | Staphylococcus aureus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus aureus | |||||||||||
CAZyme ID | MGYG000002337_01956 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | putative transglycosylase SceD | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 2089459; End: 2090154 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam06737 | Transglycosylas | 2.74e-25 | 155 | 231 | 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 | 1.91e-18 | 157 | 230 | 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 | 4.37e-06 | 177 | 219 | 50 | 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. |
cd00442 | Lyz-like | 0.010 | 162 | 194 | 5 | 38 | lysozyme-like domains. This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ANI70254.1 | 2.03e-154 | 1 | 231 | 1 | 231 |
ASI56122.1 | 2.03e-154 | 1 | 231 | 1 | 231 |
SQE67165.1 | 2.03e-154 | 1 | 231 | 1 | 231 |
VDZ93337.1 | 2.03e-154 | 1 | 231 | 1 | 231 |
AXG04224.1 | 2.03e-154 | 1 | 231 | 1 | 231 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8NVH0 | 4.74e-154 | 1 | 231 | 1 | 231 | Probable transglycosylase SceD OS=Staphylococcus aureus (strain MW2) OX=196620 GN=sceD PE=3 SV=1 |
Q2FF31 | 4.74e-154 | 1 | 231 | 1 | 231 | Probable transglycosylase SceD OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sceD PE=3 SV=1 |
Q2FWF8 | 4.74e-154 | 1 | 231 | 1 | 231 | Probable transglycosylase SceD OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sceD PE=1 SV=1 |
Q6G7L4 | 4.74e-154 | 1 | 231 | 1 | 231 | Probable transglycosylase SceD OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=sceD PE=3 SV=1 |
A6QIT9 | 4.74e-154 | 1 | 231 | 1 | 231 | Probable transglycosylase SceD OS=Staphylococcus aureus (strain Newman) OX=426430 GN=sceD PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000435 | 0.998640 | 0.000269 | 0.000235 | 0.000204 | 0.000184 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.