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CAZyme Information: MGYG000000014_04040
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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 | Clostridium butyricum | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum | |||||||||||
| CAZyme ID | MGYG000000014_04040 | |||||||||||
| CAZy Family | GH73 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 12987; End: 14999 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| NF033930 | pneumo_PspA | 2.51e-72 | 240 | 453 | 416 | 621 | pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus. |
| NF033838 | PspC_subgroup_1 | 3.85e-65 | 235 | 469 | 463 | 681 | pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. |
| cd02696 | MurNAc-LAA | 1.00e-60 | 482 | 656 | 2 | 161 | 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. |
| pfam01520 | Amidase_3 | 3.12e-56 | 482 | 648 | 1 | 154 | N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls. |
| COG0860 | AmiC | 1.41e-48 | 475 | 656 | 38 | 214 | N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AXB83718.1 | 0.0 | 1 | 670 | 1 | 670 |
| BBK78144.1 | 0.0 | 1 | 670 | 1 | 670 |
| QMW89788.1 | 0.0 | 1 | 670 | 1 | 670 |
| ALS18119.1 | 0.0 | 1 | 670 | 1 | 670 |
| AOR95193.1 | 0.0 | 1 | 670 | 1 | 670 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1JWQ_A | 6.58e-20 | 480 | 666 | 2 | 172 | Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa] |
| 4RN7_A | 3.83e-17 | 478 | 668 | 2 | 180 | ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630] |
| 5J72_A | 1.52e-15 | 472 | 651 | 444 | 618 | ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630] |
| 5EMI_A | 1.09e-14 | 477 | 666 | 1 | 174 | ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102] |
| 7RAG_B | 4.27e-14 | 478 | 662 | 15 | 201 | ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P54525 | 2.73e-19 | 480 | 666 | 30 | 200 | Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3 |
| Q02114 | 1.16e-18 | 480 | 662 | 320 | 487 | N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1 |
| Q9RMZ0 | 1.76e-17 | 480 | 648 | 333 | 498 | Uncharacterized cell wall amidase pXO2-42/BXB0045/GBAA_pXO2_0045 OS=Bacillus anthracis OX=1392 GN=pXO2-42 PE=3 SV=2 |
| Q4L6X7 | 2.38e-16 | 479 | 645 | 119 | 264 | Probable cell wall amidase LytH OS=Staphylococcus haemolyticus (strain JCSC1435) OX=279808 GN=lytH PE=3 SV=2 |
| Q8CP02 | 2.08e-14 | 480 | 645 | 120 | 264 | Probable cell wall amidase LytH OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=lytH PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000307 | 0.998955 | 0.000175 | 0.000206 | 0.000169 | 0.000155 |
