Species | UMGS1388 sp900551345 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Monoglobales; UMGS1388; UMGS1388; UMGS1388 sp900551345 | |||||||||||
CAZyme ID | MGYG000003068_00589 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 310; End: 1041 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06583 | PGRP | 1.17e-25 | 22 | 147 | 2 | 115 | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity. |
pfam01510 | Amidase_2 | 2.12e-17 | 21 | 151 | 1 | 116 | N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. |
smart00644 | Ami_2 | 6.58e-14 | 21 | 147 | 2 | 119 | Ami_2 domain. |
pfam00395 | SLH | 3.11e-11 | 190 | 230 | 1 | 42 | S-layer homology domain. |
NF033190 | inl_like_NEAT_1 | 2.60e-07 | 188 | 234 | 641 | 687 | NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CDM67796.1 | 3.22e-113 | 1 | 192 | 1 | 195 |
QAT44066.1 | 1.11e-109 | 1 | 192 | 1 | 195 |
AEY67694.1 | 3.77e-108 | 1 | 182 | 1 | 185 |
ABZ85376.1 | 8.75e-101 | 1 | 183 | 1 | 186 |
AOT72278.1 | 9.03e-101 | 1 | 182 | 1 | 188 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9RMZ0 | 7.02e-06 | 176 | 237 | 72 | 138 | Uncharacterized cell wall amidase pXO2-42/BXB0045/GBAA_pXO2_0045 OS=Bacillus anthracis OX=1392 GN=pXO2-42 PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999854 | 0.000163 | 0.000018 | 0.000001 | 0.000000 | 0.000001 |
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