Species | Corynebacterium amycolatum_A | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium amycolatum_A | |||||||||||
CAZyme ID | MGYG000001435_00373 | |||||||||||
CAZy Family | GT51 | |||||||||||
CAZyme Description | Monofunctional biosynthetic peptidoglycan transglycosylase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 440557; End: 443034 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT51 | 173 | 339 | 2.6e-62 | 0.9378531073446328 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0744 | MrcB | 1.03e-162 | 141 | 752 | 42 | 630 | Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis]. |
TIGR02074 | PBP_1a_fam | 2.29e-131 | 175 | 720 | 1 | 531 | 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 | 1.15e-98 | 138 | 732 | 29 | 733 | Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]. |
pfam00912 | Transgly | 6.35e-78 | 164 | 340 | 3 | 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. |
TIGR02071 | PBP_1b | 1.80e-66 | 137 | 697 | 92 | 670 | penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AYX80715.1 | 0.0 | 1 | 825 | 1 | 825 |
ASE56981.1 | 0.0 | 1 | 825 | 1 | 825 |
QPR31324.1 | 0.0 | 1 | 753 | 1 | 753 |
QQV00772.1 | 0.0 | 1 | 753 | 1 | 753 |
QQB83204.1 | 0.0 | 1 | 753 | 1 | 753 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5CXW_A | 4.71e-113 | 372 | 739 | 2 | 377 | Structureof the PonA1 protein from Mycobacterium Tuberculosis in complex with penicillin V [Mycobacterium tuberculosis H37Rv] |
5CRF_A | 9.05e-109 | 372 | 739 | 2 | 377 | Structureof the penicillin-binding protein PonA1 from Mycobacterium Tuberculosis [Mycobacterium tuberculosis H37Rv],5CRF_B Structure of the penicillin-binding protein PonA1 from Mycobacterium Tuberculosis [Mycobacterium tuberculosis H37Rv],5CRF_C Structure of the penicillin-binding protein PonA1 from Mycobacterium Tuberculosis [Mycobacterium tuberculosis H37Rv],5CRF_D Structure of the penicillin-binding protein PonA1 from Mycobacterium Tuberculosis [Mycobacterium tuberculosis H37Rv] |
3ZG8_B | 1.17e-46 | 259 | 685 | 2 | 431 | CrystalStructure of Penicillin Binding Protein 4 from Listeria monocytogenes in the Ampicillin bound form [Listeria monocytogenes],3ZG9_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Cefuroxime bound form [Listeria monocytogenes],3ZGA_B Crystal Structure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the Carbenicillin bound form [Listeria monocytogenes] |
2JE5_A | 3.34e-44 | 134 | 697 | 8 | 618 | 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] |
3ZG7_B | 2.39e-43 | 259 | 685 | 2 | 431 | CrystalStructure of Penicillin-Binding Protein 4 from Listeria monocytogenes in the apo form [Listeria monocytogenes] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A0R7G2 | 3.21e-219 | 121 | 750 | 77 | 716 | Penicillin-binding protein 1A OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ponA1 PE=3 SV=1 |
P71707 | 1.20e-202 | 111 | 739 | 129 | 767 | Penicillin-binding protein 1A OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=ponA1 PE=1 SV=3 |
Q8DNB6 | 1.51e-56 | 114 | 685 | 56 | 622 | Penicillin-binding protein 2a OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pbp2a PE=1 SV=1 |
A0A0H2ZMF9 | 1.51e-56 | 114 | 685 | 56 | 622 | Penicillin-binding protein 2a OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=pbp2a PE=1 SV=1 |
P38050 | 1.23e-52 | 157 | 732 | 51 | 610 | Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000033 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.