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CAZyme Information: MGYG000002305_02760

You are here: Home > Sequence: MGYG000002305_02760

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 Leminorella grimontii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Leminorella; Leminorella grimontii
CAZyme ID MGYG000002305_02760
CAZy Family CBM50
CAZyme Description N-acetylmuramoyl-L-alanine amidase AmiB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
528 56172.72 10.5988
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002305 4219592 Isolate not provided not provided
Gene Location Start: 127369;  End: 128955  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002305_02760.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10431 PRK10431 0.0 45 462 27 442
N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860 AmiC 1.22e-72 184 436 15 228
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696 MurNAc-LAA 2.91e-60 213 432 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 7.03e-56 191 436 36 276
N-acetylmuramoyl-L-alanine amidase AmiA.
pfam01520 Amidase_3 6.67e-53 214 432 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
AKJ41024.1 1.84e-247 19 527 1 507
VEJ53290.1 1.68e-245 19 527 1 506
QBH95214.1 1.25e-243 19 527 1 520
AWH90083.1 2.11e-236 22 527 1 516
QCR03247.1 2.43e-183 31 522 13 500

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 4.02e-47 44 436 23 393
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 9.96e-29 214 435 7 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 9.54e-26 208 435 1 177
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A 6.43e-20 213 435 3 175
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A 8.25e-16 214 438 6 184
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
P26366 1.91e-155 32 454 14 428
N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P26365 8.72e-153 32 450 14 429
N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P44493 9.10e-88 212 528 23 345
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 8.22e-48 211 436 4 228
Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
P63884 5.80e-47 20 436 11 407
N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=amiC 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
0.055496 0.940715 0.002681 0.000487 0.000300 0.000298

TMHMM  Annotations      download full data without filtering help

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