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CAZyme Information: MGYG000000147_00547

You are here: Home > Sequence: MGYG000000147_00547

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 Bacillus paralicheniformis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus paralicheniformis
CAZyme ID MGYG000000147_00547
CAZy Family CBM50
CAZyme Description Putative L,D-transpeptidase YkuD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
165 17965.73 10.6657
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000147 4371304 Isolate United Kingdom Europe
Gene Location Start: 531743;  End: 532240  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000147_00547.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16913 YkuD_like 3.80e-39 58 164 1 121
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.
COG1376 ErfK 8.85e-27 11 164 46 229
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis].
pfam03734 YkuD 3.00e-22 56 163 1 89
L,D-transpeptidase catalytic domain. This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.
PRK10260 PRK10260 7.81e-17 12 161 53 231
L,D-transpeptidase; Provisional
PRK10190 PRK10190 2.21e-16 12 163 50 230
L,D-transpeptidase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QEO06804.1 2.02e-117 1 165 1 165
QFY39171.1 2.02e-117 1 165 1 165
AYQ16068.1 2.02e-117 1 165 1 165
ARA85407.1 2.02e-117 1 165 1 165
QSF98361.1 2.02e-117 1 165 1 165

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2MTZ_A 7.51e-87 1 163 4 165
Haddockmodel of Bacillus subtilis L,D-transpeptidase in complex with a peptidoglycan hexamuropeptide [Bacillus subtilis],3ZQD_A B. subtilis L,D-transpeptidase [Bacillus subtilis subsp. subtilis str. 168],4A52_A NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
4A1I_A 1.26e-85 1 163 2 163
ykudfrom B.subtilis [Bacillus subtilis],4A1I_B ykud from B.subtilis [Bacillus subtilis],4A1I_C ykud from B.subtilis [Bacillus subtilis],4A1I_D ykud from B.subtilis [Bacillus subtilis],4A1I_E ykud from B.subtilis [Bacillus subtilis],4A1I_F ykud from B.subtilis [Bacillus subtilis],4A1I_G ykud from B.subtilis [Bacillus subtilis],4A1I_H ykud from B.subtilis [Bacillus subtilis],4A1J_A Ykud L,D-transpeptidase from B.subtilis [Bacillus subtilis],4A1J_B Ykud L,D-transpeptidase from B.subtilis [Bacillus subtilis]
4A1K_A 4.20e-84 1 163 2 163
YkudL,D-transpeptidase [Bacillus subtilis]
1Y7M_A 8.19e-84 2 163 2 162
ChainA, Crystal Structure of the B. subtilis YkuD protein at 2 A resolution [Bacillus subtilis subsp. subtilis str. 168],1Y7M_B Chain B, Crystal Structure of the B. subtilis YkuD protein at 2 A resolution [Bacillus subtilis subsp. subtilis str. 168]
4LZH_A 6.64e-13 10 161 30 210
ChainA, L,D-transpeptidase [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q65K99 6.20e-113 1 165 1 165
Putative L,D-transpeptidase YkuD OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi01617 PE=3 SV=1
O34816 9.91e-87 1 163 1 162
Putative L,D-transpeptidase YkuD OS=Bacillus subtilis (strain 168) OX=224308 GN=ykuD PE=1 SV=1
Q5WC42 6.34e-74 1 165 1 165
Putative L,D-transpeptidase YkuD OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=ABC3535 PE=3 SV=1
P54539 2.90e-20 56 164 27 151
Putative L,D-transpeptidase YqjB OS=Bacillus subtilis (strain 168) OX=224308 GN=yqjB PE=3 SV=1
P39176 1.53e-17 10 163 48 230
Probable L,D-transpeptidase ErfK/SrfK OS=Escherichia coli (strain K12) OX=83333 GN=erfK PE=1 SV=2

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
0.999495 0.000503 0.000025 0.000001 0.000001 0.000003

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000147_00547.