Species | Fenollaria sp900539225 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Fenollaria; Fenollaria sp900539225 | |||||||||||
CAZyme ID | MGYG000000766_01019 | |||||||||||
CAZy Family | GT51 | |||||||||||
CAZyme Description | Monofunctional biosynthetic peptidoglycan transglycosylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 82399; End: 85371 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT51 | 71 | 230 | 3.6e-63 | 0.8926553672316384 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR02074 | PBP_1a_fam | 5.50e-166 | 81 | 812 | 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 | 1.58e-157 | 7 | 866 | 2 | 654 | Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis]. |
COG5009 | MrcA | 3.57e-157 | 26 | 869 | 10 | 772 | Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]. |
PRK11636 | mrcA | 1.51e-75 | 65 | 862 | 50 | 829 | penicillin-binding protein 1a; Provisional |
pfam00912 | Transgly | 1.99e-75 | 69 | 230 | 1 | 161 | 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 |
---|---|---|---|---|---|
AVM66314.1 | 0.0 | 1 | 957 | 1 | 955 |
SHD77321.1 | 0.0 | 3 | 962 | 4 | 943 |
QAT62113.1 | 0.0 | 35 | 939 | 34 | 931 |
QQY80508.1 | 0.0 | 41 | 920 | 48 | 927 |
QIB26572.1 | 2.07e-294 | 31 | 939 | 30 | 937 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7U4H_A | 6.64e-228 | 47 | 920 | 5 | 866 | 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] |
4OON_A | 9.37e-69 | 65 | 836 | 23 | 748 | 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] |
5U2G_A | 4.67e-61 | 65 | 889 | 24 | 837 | 2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20] |
3UDF_A | 4.21e-55 | 65 | 787 | 23 | 691 | ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii] |
2JE5_A | 6.55e-46 | 69 | 841 | 41 | 668 | 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 |
---|---|---|---|---|---|---|
Q891X1 | 1.12e-109 | 1 | 879 | 1 | 721 | Penicillin-binding protein 1A OS=Clostridium tetani (strain Massachusetts / E88) OX=212717 GN=pbpA PE=3 SV=1 |
A7GHV1 | 1.94e-109 | 5 | 895 | 3 | 729 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) OX=441772 GN=pbpA PE=3 SV=1 |
Q0TNZ8 | 1.52e-108 | 36 | 883 | 46 | 744 | 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 |
A5I6G4 | 7.91e-108 | 5 | 895 | 3 | 729 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) OX=441771 GN=pbpA PE=3 SV=1 |
A7FY32 | 7.91e-108 | 5 | 895 | 3 | 729 | Penicillin-binding protein 1A OS=Clostridium botulinum (strain ATCC 19397 / Type A) OX=441770 GN=pbpA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.935552 | 0.050196 | 0.000669 | 0.000295 | 0.000155 | 0.013147 |
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