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CAZyme Information: MGYG000002373_01921

You are here: Home > Sequence: MGYG000002373_01921

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 septicum
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium septicum
CAZyme ID MGYG000002373_01921
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1105 MGYG000002373_22|CGC1 120713.41 6.7491
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002373 3298966 Isolate France Europe
Gene Location Start: 46415;  End: 49732  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002373_01921.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 1.58e-50 894 1102 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.
pfam01520 Amidase_3 5.16e-43 895 1099 1 170
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 4.30e-41 893 1105 43 228
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
smart00646 Ami_3 4.37e-25 965 1099 1 111
Ami_3 domain.
PRK10319 PRK10319 2.89e-21 888 1105 52 276
N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYE34895.1 0.0 1 1105 1 1333
QAS60290.1 0.0 1 1105 1 1561
QLY79091.1 1.44e-138 221 931 48 759
AGK55741.1 2.23e-111 212 898 44 716
CCO12189.2 8.94e-101 210 1105 609 1472

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4RN7_A 3.18e-16 895 1101 6 178
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A 2.58e-14 893 1103 2 174
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A 2.26e-13 894 1103 6 176
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
7RAG_B 6.51e-13 892 1103 16 207
ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]
3NE8_A 2.17e-12 889 1105 1 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54525 7.87e-20 893 1105 30 204
Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q02114 5.99e-17 862 1105 288 495
N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P36548 1.09e-15 888 1105 52 276
N-acetylmuramoyl-L-alanine amidase AmiA OS=Escherichia coli (strain K12) OX=83333 GN=amiA PE=1 SV=1
P33772 5.24e-14 888 1105 52 276
N-acetylmuramoyl-L-alanine amidase AmiA OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiA PE=3 SV=1
Q49Y70 7.26e-14 869 1105 84 289
Probable cell wall amidase LytH OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 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
0.000430 0.998828 0.000196 0.000188 0.000171 0.000157

TMHMM  Annotations      download full data without filtering help

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