| Species | Enterococcus_C asini | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_C; Enterococcus_C asini | |||||||||||
| CAZyme ID | MGYG000000163_01459 | |||||||||||
| CAZy Family | GT51 | |||||||||||
| CAZyme Description | Monofunctional biosynthetic peptidoglycan transglycosylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 203205; End: 205685 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT51 | 90 | 275 | 1.2e-52 | 0.9774011299435028 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG0744 | MrcB | 2.97e-141 | 33 | 686 | 9 | 600 | Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis]. |
| COG5009 | MrcA | 2.22e-76 | 33 | 735 | 7 | 767 | Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]. |
| pfam00912 | Transgly | 4.43e-60 | 88 | 276 | 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 | 2.35e-54 | 82 | 723 | 36 | 597 | Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis]. |
| PRK11636 | mrcA | 1.53e-43 | 33 | 676 | 7 | 757 | penicillin-binding protein 1a; Provisional |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCA85367.1 | 0.0 | 1 | 784 | 1 | 783 |
| AYY11009.1 | 0.0 | 1 | 768 | 1 | 767 |
| QOG27803.1 | 0.0 | 1 | 768 | 1 | 767 |
| QGR81606.1 | 0.0 | 1 | 768 | 1 | 767 |
| QCT93040.1 | 0.0 | 1 | 768 | 1 | 767 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2JE5_A | 1.46e-217 | 49 | 770 | 2 | 717 | 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 | 8.73e-122 | 294 | 770 | 24 | 491 | 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 | 8.73e-122 | 294 | 770 | 24 | 491 | 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 | 1.73e-121 | 294 | 770 | 24 | 491 | 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 | 4.81e-121 | 294 | 770 | 24 | 491 | 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 |
|---|---|---|---|---|---|---|
| Q0SRL7 | 2.42e-58 | 84 | 661 | 73 | 641 | Penicillin-binding protein 1A OS=Clostridium perfringens (strain SM101 / Type A) OX=289380 GN=pbpA PE=3 SV=1 |
| Q0TNZ8 | 3.14e-57 | 38 | 719 | 33 | 693 | Penicillin-binding protein 1A OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=pbpA PE=3 SV=1 |
| Q8XJ01 | 6.33e-56 | 38 | 686 | 33 | 661 | Penicillin-binding protein 1A OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=pbpA PE=3 SV=1 |
| A0A0H2ZMF9 | 7.14e-56 | 41 | 730 | 59 | 688 | Penicillin-binding protein 2a OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=pbp2a PE=1 SV=1 |
| Q8DNB6 | 7.14e-56 | 41 | 730 | 59 | 688 | Penicillin-binding protein 2a OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pbp2a PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.999819 | 0.000181 | 0.000001 | 0.000001 | 0.000000 | 0.000002 |
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