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CAZyme Information: MGYG000002466_02023

You are here: Home > Sequence: MGYG000002466_02023

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 Yersinia frederiksenii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia frederiksenii
CAZyme ID MGYG000002466_02023
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
636 68440.47 10.837
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002466 4803605 Isolate Finland Europe
Gene Location Start: 99988;  End: 101898  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002466_02023.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10431 PRK10431 0.0 25 478 8 426
N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860 AmiC 6.11e-73 233 471 32 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696 MurNAc-LAA 5.75e-60 245 464 1 171
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.
PRK10319 PRK10319 5.12e-57 213 468 28 276
N-acetylmuramoyl-L-alanine amidase AmiA.
pfam01520 Amidase_3 2.38e-52 246 464 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATM98171.1 0.0 26 636 1 611
QAX81039.1 0.0 26 636 1 610
AHM76059.2 0.0 26 636 1 610
CBY28922.1 0.0 1 636 1 645
VEA98083.1 0.0 1 636 1 645

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 5.01e-44 40 468 20 393
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 8.87e-24 246 467 7 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 2.13e-21 241 467 2 177
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A 2.51e-16 245 467 3 175
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A 7.64e-14 241 467 1 181
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26365 2.42e-164 39 478 22 426
N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P26366 8.99e-163 39 478 22 420
N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P44493 7.58e-88 244 633 23 429
Probable N-acetylmuramoyl-L-alanine amidase AmiB OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=amiB PE=3 SV=1
P57638 1.53e-54 241 468 2 228
Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
Q8K908 1.43e-50 248 468 2 222
Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=amiB 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
0.000480 0.998549 0.000327 0.000230 0.000195 0.000169

TMHMM  Annotations      download full data without filtering help

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