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CAZyme Information: MGYG000003012_01579
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Blautia_A sp900540785 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900540785 | |||||||||||
| CAZyme ID | MGYG000003012_01579 | |||||||||||
| CAZy Family | GH73 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 13063; End: 14451 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd02696 | MurNAc-LAA | 8.80e-26 | 180 | 354 | 2 | 167 | N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall. |
| COG0860 | AmiC | 5.95e-13 | 185 | 354 | 50 | 220 | N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis]. |
| pfam01832 | Glucosaminidase | 7.63e-10 | 36 | 102 | 2 | 77 | Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan. |
| COG3409 | PGRP | 1.63e-04 | 373 | 461 | 19 | 104 | Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis]. |
| pfam01471 | PG_binding_1 | 8.30e-04 | 402 | 457 | 7 | 55 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QJU16443.1 | 1.25e-95 | 1 | 368 | 1 | 358 |
| QMW80642.1 | 1.50e-94 | 1 | 411 | 1 | 382 |
| QMW77672.1 | 1.09e-93 | 1 | 411 | 1 | 382 |
| QIB56084.1 | 1.09e-93 | 1 | 411 | 1 | 382 |
| AFC63685.1 | 1.09e-71 | 3 | 169 | 203 | 369 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3QAY_A | 9.65e-51 | 178 | 360 | 2 | 180 | ChainA, Endolysin [Clostridium virus phiCD27],3QAY_B Chain B, Endolysin [Clostridium virus phiCD27],3QAY_C Chain C, Endolysin [Clostridium virus phiCD27],3QAY_D Chain D, Endolysin [Clostridium virus phiCD27] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O51481 | 4.29e-25 | 5 | 167 | 41 | 196 | Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1 |
| P58698 | 3.93e-09 | 205 | 359 | 20 | 178 | Uncharacterized protein CPE1502 OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=CPE1502 PE=4 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000056 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |