Species | Enterococcus_B faecium | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B faecium | |||||||||||
CAZyme ID | MGYG000002353_02017 | |||||||||||
CAZy Family | GT51 | |||||||||||
CAZyme Description | Penicillin-binding protein 1A/1B | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2053406; End: 2055751 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT51 | 88 | 273 | 3.5e-50 | 0.9774011299435028 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0744 | MrcB | 7.12e-150 | 33 | 727 | 14 | 640 | Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis]. |
COG5009 | MrcA | 3.79e-89 | 34 | 662 | 7 | 697 | Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]. |
pfam00912 | Transgly | 2.67e-59 | 86 | 274 | 1 | 177 | Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains. |
COG4953 | PbpC | 8.70e-55 | 83 | 684 | 49 | 560 | Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis]. |
PRK11636 | mrcA | 1.13e-47 | 39 | 658 | 7 | 745 | penicillin-binding protein 1a; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
VFA47939.1 | 0.0 | 1 | 781 | 1 | 781 |
QPQ19194.1 | 0.0 | 1 | 781 | 1 | 781 |
QDA52998.1 | 0.0 | 1 | 781 | 1 | 781 |
AOM15192.1 | 0.0 | 1 | 781 | 1 | 781 |
QUU14099.1 | 0.0 | 1 | 781 | 1 | 781 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2JE5_A | 3.88e-222 | 46 | 762 | 1 | 714 | StructuralAnd Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6],2JE5_B Structural And Mechanistic Basis Of Penicillin Binding Protein Inhibition By Lactivicins [Streptococcus pneumoniae R6] |
2BG1_A | 1.76e-123 | 292 | 762 | 24 | 488 | Activesite restructuring regulates ligand recognition in classA Penicillin-binding proteins (PBPs) [Streptococcus pneumoniae R6],2XD5_A Structural insights into the catalytic mechanism and the role of Streptococcus pneumoniae PBP1b [Streptococcus pneumoniae R6],2XD5_B Structural insights into the catalytic mechanism and the role of Streptococcus pneumoniae PBP1b [Streptococcus pneumoniae R6] |
2XD1_A | 1.76e-123 | 292 | 762 | 24 | 488 | ACTIVESITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASS A PENICILLIN-BINDING PROTEINS [Streptococcus pneumoniae R6],2XD1_B ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASS A PENICILLIN-BINDING PROTEINS [Streptococcus pneumoniae R6] |
2Y2G_A | 3.48e-123 | 292 | 762 | 24 | 488 | Penicillin-BindingProtein 1b (Pbp-1b) In Complex With An Alkyl Boronate (A01) [Streptococcus pneumoniae R6],2Y2G_B Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (A01) [Streptococcus pneumoniae R6],2Y2H_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za2) [Streptococcus pneumoniae R6],2Y2H_B Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za2) [Streptococcus pneumoniae R6],2Y2I_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za3) [Streptococcus pneumoniae R6],2Y2J_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za4) [Streptococcus pneumoniae R6],2Y2K_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Za5) [Streptococcus pneumoniae R6],2Y2L_A Penicillin-binding Protein 1b (pbp-1b) In Complex With An Alkyl Boronate (e06) [Streptococcus pneumoniae R6],2Y2L_B Penicillin-binding Protein 1b (pbp-1b) In Complex With An Alkyl Boronate (e06) [Streptococcus pneumoniae R6],2Y2M_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (E08) [Streptococcus pneumoniae R6],2Y2N_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (E07) [Streptococcus pneumoniae R6],2Y2O_A Penicillin-binding Protein 1b (pbp-1b) In Complex With An Alkyl Boronate (eo9) [Streptococcus pneumoniae R6],2Y2P_A Penicillin-binding protein 1b (pbp-1b) in complex with an alkyl boronate (z10) [Streptococcus pneumoniae R6],2Y2Q_A Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Z06) [Streptococcus pneumoniae R6],2Y2Q_B Penicillin-Binding Protein 1b (Pbp-1b) In Complex With An Alkyl Boronate (Z06) [Streptococcus pneumoniae R6] |
2UWX_A | 9.72e-123 | 292 | 762 | 24 | 488 | Activesite restructuring regulates ligand recognition in class A penicillin-binding proteins [Streptococcus pneumoniae R6] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A5I6G4 | 8.80e-52 | 12 | 663 | 4 | 625 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1 |
A7FY32 | 8.80e-52 | 12 | 663 | 4 | 625 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1 |
A7GHV1 | 2.12e-51 | 12 | 663 | 4 | 625 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1 |
P39793 | 5.58e-50 | 39 | 659 | 41 | 617 | Penicillin-binding protein 1A/1B OS=Bacillus subtilis (strain 168) OX=224308 GN=ponA PE=1 SV=1 |
Q0SRL7 | 1.82e-49 | 7 | 683 | 4 | 667 | Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 GN=pbpA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000011 | 0.000027 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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