Species | Ruminococcus_E sp900543095 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp900543095 | |||||||||||
CAZyme ID | MGYG000002263_00535 | |||||||||||
CAZy Family | GT51 | |||||||||||
CAZyme Description | Monofunctional glycosyltransferase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 50588; End: 52987 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT51 | 99 | 271 | 3.5e-65 | 0.9717514124293786 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR02074 | PBP_1a_fam | 3.53e-135 | 107 | 667 | 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] |
COG0744 | MrcB | 1.75e-129 | 28 | 671 | 2 | 603 | Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis]. |
COG5009 | MrcA | 8.71e-106 | 39 | 691 | 3 | 745 | Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]. |
pfam00912 | Transgly | 5.22e-79 | 103 | 271 | 8 | 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 | 5.56e-56 | 108 | 642 | 58 | 537 | Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QCT07186.1 | 6.49e-288 | 5 | 726 | 45 | 759 |
CAB1249043.1 | 1.90e-201 | 5 | 712 | 2 | 699 |
QEY34222.1 | 4.02e-201 | 5 | 712 | 2 | 698 |
QNK41697.1 | 5.57e-194 | 5 | 728 | 2 | 719 |
QAT49292.1 | 7.10e-193 | 5 | 731 | 2 | 722 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7U4H_A | 2.53e-53 | 75 | 712 | 8 | 808 | ChainA, Penicillin-binding protein 1A (Pbp1a) [Chlamydia trachomatis D/UW-3/CX],7U4H_B Chain B, Penicillin-binding protein 1A (Pbp1a) [Chlamydia trachomatis D/UW-3/CX] |
3DWK_A | 9.51e-48 | 86 | 641 | 10 | 557 | ChainA, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_B Chain B, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_C Chain C, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL],3DWK_D Chain D, Penicillin-binding protein 2 [Staphylococcus aureus subsp. aureus COL] |
4OON_A | 5.61e-47 | 115 | 712 | 46 | 770 | Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1] |
2OLU_A | 1.86e-43 | 86 | 641 | 19 | 566 | StructuralInsight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Apoenzyme [Staphylococcus aureus],2OLV_A Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus],2OLV_B Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex [Staphylococcus aureus] |
2JE5_A | 7.61e-42 | 108 | 648 | 54 | 614 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8XJ01 | 2.49e-80 | 4 | 662 | 5 | 663 | Penicillin-binding protein 1A OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=pbpA PE=3 SV=1 |
A7GHV1 | 1.21e-79 | 54 | 700 | 26 | 669 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1 |
A5I6G4 | 2.44e-79 | 54 | 700 | 26 | 669 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1 |
A7FY32 | 2.44e-79 | 54 | 700 | 26 | 669 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1 |
Q0SRL7 | 5.42e-79 | 12 | 672 | 8 | 673 | 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 |
---|---|---|---|---|---|
0.999897 | 0.000107 | 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.