Species | Lactobacillus paragasseri | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus paragasseri | |||||||||||
CAZyme ID | MGYG000002387_00473 | |||||||||||
CAZy Family | GT51 | |||||||||||
CAZyme Description | Monofunctional biosynthetic peptidoglycan transglycosylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 454762; End: 457590 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT51 | 102 | 288 | 7.8e-53 | 0.9774011299435028 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0744 | MrcB | 1.03e-145 | 42 | 772 | 9 | 661 | Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis]. |
TIGR02074 | PBP_1a_fam | 4.01e-132 | 119 | 710 | 9 | 530 | penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan] |
COG5009 | MrcA | 8.88e-93 | 47 | 683 | 7 | 695 | Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]. |
COG4953 | PbpC | 6.46e-78 | 119 | 726 | 65 | 565 | Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis]. |
pfam00912 | Transgly | 1.95e-65 | 118 | 288 | 19 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QTP20030.1 | 0.0 | 1 | 942 | 1 | 942 |
ART97821.1 | 0.0 | 1 | 942 | 1 | 942 |
QHC52691.1 | 0.0 | 1 | 942 | 1 | 942 |
QTD66155.1 | 0.0 | 1 | 942 | 1 | 942 |
BBD48082.1 | 0.0 | 1 | 942 | 1 | 942 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2JE5_A | 5.07e-140 | 61 | 791 | 3 | 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] |
2FFF_B | 3.28e-68 | 325 | 791 | 2 | 452 | OpenForm of a Class A Transpeptidase Domain [Streptococcus pneumoniae] |
2BG1_A | 4.90e-68 | 325 | 791 | 41 | 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 | 4.90e-68 | 325 | 791 | 41 | 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] |
2UWX_A | 2.43e-67 | 325 | 791 | 41 | 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 |
---|---|---|---|---|---|---|
P38050 | 6.99e-68 | 116 | 680 | 71 | 571 | Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2 |
P40750 | 1.73e-59 | 124 | 709 | 88 | 624 | Penicillin-binding protein 4 OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpD PE=1 SV=2 |
A7GHV1 | 3.48e-58 | 124 | 746 | 88 | 676 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1 |
A7FY32 | 1.62e-57 | 124 | 746 | 88 | 676 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1 |
A5I6G4 | 1.62e-57 | 124 | 746 | 88 | 676 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999884 | 0.000125 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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