logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000113_00423

You are here: Home > Sequence: MGYG000000113_00423

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 Streptococcus salivarius
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus salivarius
CAZyme ID MGYG000000113_00423
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
708 MGYG000000113_2|CGC3 76965.26 5.0718
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000113 2251845 Isolate Canada North America
Gene Location Start: 181022;  End: 183148  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000113_00423.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 134 267 1.7e-35 0.9296875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 4.44e-71 512 699 1 172
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 7.01e-66 476 704 13 230
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520 Amidase_3 1.08e-61 513 698 1 172
N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG1705 FlgJ 1.93e-55 92 279 11 196
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
TIGR02883 spore_cwlD 1.09e-41 511 701 1 189
N-acetylmuramoyl-L-alanine amidase CwlD. Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QMI50933.1 0.0 1 708 1 708
ARC22385.1 0.0 1 708 1 708
ARC34284.1 0.0 1 708 1 708
QEM32624.1 0.0 1 708 1 708
ALR79867.1 0.0 1 708 1 708

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1JWQ_A 1.74e-30 511 703 2 177
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A 1.44e-29 513 705 6 185
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
3FI7_A 1.89e-23 120 271 30 183
CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e]
5EMI_A 1.11e-22 512 704 6 180
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
5DN4_A 2.14e-21 136 283 20 165
Structureof the glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54525 3.01e-35 508 704 27 206
Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
O32083 1.49e-31 112 287 41 214
Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
Q02114 1.60e-27 508 702 317 495
N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q06320 5.92e-26 513 702 4 175
Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
Q8CP02 9.51e-26 511 702 120 289
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
0.002417 0.992148 0.004762 0.000222 0.000207 0.000202

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000113_00423.