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CAZyme Information: MGYG000002423_00140

You are here: Home > Sequence: MGYG000002423_00140

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 Pantoea septica
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Pantoea; Pantoea septica
CAZyme ID MGYG000002423_00140
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
552 59024.28 10.8048
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002423 4877109 Isolate United States North America
Gene Location Start: 109979;  End: 111637  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002423_00140.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10431 PRK10431 0.0 1 440 1 440
N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860 AmiC 1.84e-70 188 414 44 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
PRK10319 PRK10319 2.12e-60 161 411 35 276
N-acetylmuramoyl-L-alanine amidase AmiA.
cd02696 MurNAc-LAA 4.71e-57 188 407 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.
pfam01520 Amidase_3 6.93e-49 189 407 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
QGR08230.1 3.08e-312 1 552 1 549
ALV90866.1 3.44e-312 1 552 1 552
QCP61021.1 5.69e-311 1 552 1 552
ADU70851.1 4.16e-310 1 552 1 549
QGY56826.1 3.12e-309 1 552 1 556

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 4.25e-45 28 411 25 393
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 2.23e-28 183 410 1 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 2.06e-20 187 410 5 177
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A 2.07e-18 188 410 3 175
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
7RAG_B 7.25e-15 181 410 13 208
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
P26366 8.17e-181 1 421 1 420
N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P26365 3.80e-178 1 421 1 426
N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P44493 1.73e-91 187 549 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 2.36e-56 187 411 5 228
Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
Q8K908 1.36e-51 191 419 2 230
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
0.000278 0.998998 0.000183 0.000178 0.000164 0.000149

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002423_00140.