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BACAN:Q81YZ2

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Species (Taxon ID) Bacillus anthracis. (1392)
Gene Name(s) yegX (ECO:0000313 with EMBL:BAR78738.1)
Protein Name(s) Endolysin (ECO:0000313 with EMBL:BAR78738.1)

N-acetylmuramoyl-L-alanine amidase (ECO:0000313 with EMBL:APT24131.1) Putative prophage LambdaBa04, glycosyl hydrolase, family 25 (ECO:0000313 with EMBL:AAT29579.1)

External Links
UniProt Q81YZ2
EMBL AE017334
CP018903
AP014833
RefSeq WP_000509854.1
PDB 3HMC
PDBsum 3HMC
STRING 198094.BA_0485
CAZy GH25
DNASU 1088730
EnsemblBacteria AAT29579
AJH86633
KOM62985
KOM67847
KOM70346
KOM81313
KOM92796
KON03452
KON16678
KON25403
KOR61324
KOR65889
KEGG banh:HYU01_02600
bar:GBAA_0485
eggNOG ENOG4108ZWG
COG3757
HOGENOM HOG000091889
OMA VLDISEW
Proteomes UP000000594
UP000185489
GO GO:0003796
GO:0005975
GO:0016998
GO:0009253
Gene3D 3.20.20.80
InterPro IPR021976
IPR002053
IPR013781
IPR017853
Pfam PF12123
PF01183
SUPFAM SSF51445

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003796

lysozyme activity

PMID:21816821[1]

ECO:0000314

F

Figure 3A shows the bactericidal activity of lysin XlyA against B. cereus and B. subtillis. Figure 3C illustrates the residues of the XlyA catalytic domain. It is shown in this figure some structures present in the XylA catalytic domain are identical to those of PlyL, another endolysin.

complete
CACAO 12602

GO:0003796

lysozyme activity

PMID:21816821[1]

ECO:0000247

PMID:3190764[2]


F

Figure 3B shows the sequence of the XlyA catalytic domain is similar to the catalytic domain of PlyL, another endolysin. The red boxes show XlyA contains catalytic and substrate recognition residues similar or identical to PlyL.The asterisks indicate base pair identity between XlyA and PlyL sequences. The colons indicate base pair similarity between XylA and PlyL. The high similarity and identity within the sequence alignment and secondary structure assignments of XylA and PlyL support the lysozyme function of XylA.

complete
CACAO 12603

GO:0003796

lysozyme activity

PMID:21816821[1]

ECO:0000250

UniProtKB:Q81YZ2


F

Figure 2B shows the structural homolog of XlyA. XlyA is an endolysin. Figure 2B shows structural similarity between XlyA and another amidase lysin, PlyL.

complete
CACAO 12636

GO:0016998

cell wall macromolecule catabolic process

PMID:21816821[1]

ECO:0000314

P

The effect of B-anthracis s-layer on lytic activity and whole cell binding by using two homologous amidases plyL and plyG are show in these figures. Figure 5A: shows the pulling down of whole cell wall binding assay using a tagged CBD of plyL and plyG infecting wild B. anthracis, B. cereus 4342 B. and subtilis. Also using it as a control as a architecture. Lower gels are Western blots using anti-His antibody, and the Upper gels show expression of Sap protein, with markers at 59 and 107 kDa.

complete
CACAO 12639

GO:0003796

lysozyme activity

PMID:21816821[1]

ECO:0000250

F

In Figure 2A, both XylA and PlyL’s structures were being compared which indicated that the two of these proteins are amidase lysins. In this particular figure(2A), their functions were being tested based on their ability to lyse B. Subtilis. They found that the catalytic domain of PlyL which was indicated in the paper by “PlyL CAT” had homologous lysing abilities to the entirety of XylA.

Missing: with/from
CACAO 12646

GO:0005975

carbohydrate metabolic process

PMID:21816821[1]

ECO:0000314

P

Figure 1 shows the use of carboxyl groups on MurNac moiety to for an amide bond with α-amino group of l-Ala. The chemical reaction's use of the carboxyl groups to form additional bonds between peptides.

complete
CACAO 12662

GO:0016998

cell wall macromolecule catabolic process

PMID:21816821[1]

ECO:0000314

P

the Effect of S-layer—Was compared the effects of PlyL and they were closely related PlyG with 96% identical in the catalytic domain , and 63% in the CBD. Figure 5A: shows how the cell killing activity of the full length which is the top bar and the catalytic domain the second bar of plyL and plyG against B. anthracis Sterne, B. anthracis (sap) mutant deficient in S-layer synthesis,and B. subtilis. Each B strains consist of 0.4uM of lysin concentration. From the graph we can also conclude that PlyG(CAT) killed Sterne more than twice as fast as PlyG(FULL). The full length graph show that with out S-layer, PlyL and plyG can still be active. The blue bar is plyL (full) and red bar is plyL(CAT). the light blue bar is plyG (full) and green bar is plyG(CAT). PlyL(CAT) had a higher lytic activity than PlyL(FULL), and PlyG(CAT) killed Sterne more than twice as fast as PlyG (FULL)

complete
CACAO 12887

GO:0003796

lysozyme activity

PMID:21816821[1]

ECO:0000314

F

Figure 1 displays that the two glycan chains are cross-peptide linked. The bond formed is what the amidase lysins target . It displays the cleavage positions of other common lysins in comparison to this lysin. Through this figure one can see that the gram-positive bacteria displays species as well as strain specific "secondary cell wall polymers" (SCWPS). These insert themselves into the lipid bilayer, which changes the appearance and the charge of the outer envelope. Figure 2 was used in order to compare this lysin to two homologous amidase lysins to see the similar structures and distinct behaviours between them (PlyL and XlyA). Due to the high structural similarity, a test was conducted to see whether the innate catalytic acitivty of XlyA was similar to that of PlyL. Figure 3 displays that XlyA:plyL chimera failed to lyse B. subtilis, however it did lyse B. cereus.

complete
CACAO 12909

GO:0016787

hydrolase activity

PMID:21816821[1]

ECO:0000314

F

Figure 4C shows the four mutation sites in PlyBa04. In addition, a glycan muropeptide fragment is shown, connecting it to pneumococcal phage lysin. The PlyBa04 (blue) and PlyB (gray) catalytic domains are identified, showing their similarity using heavy atom methods. They are glycosyl hydrolases, having a mostly parallel central eight-stranded beta-barrel with a helix/extended loop connected the rest of the seven parallel strands. The seventh and eighth strands are connected by a short beta-hairpin, creating the anti parallel strand.

complete
CACAO 12914

GO:0016787

hydrolase activity

PMID:21816821[1]

ECO:0000314

F

In Figure 1, SCWPs are typically attached via the C-6 hydroxyl group on MurNac. The presence of the hydroxyl group is indication of hydrolase activity. The d-Glu uses its γ-carboxyl to makes an amide bond with m-DAP. The presence of a carboxyl group, which contains bonds used in hydrolase activity. The γ-carboxyl is used similarly to an enzyme in the process of making an amide bond.

complete
CACAO 12918

enables

GO:0003796

lysozyme activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002053

F

Seeded From UniProt

complete

involved_in

GO:0009253

peptidoglycan catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002053

P

Seeded From UniProt

complete

involved_in

GO:0016998

cell wall macromolecule catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002053

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 Low, LY et al. (2011) Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins. J. Biol. Chem. 286 34391-403 PubMed GONUTS page
  2. Andreuccetti, D et al. (1988) Analysis of electric and magnetic fields leaking from induction heaters. Bioelectromagnetics 9 373-9 PubMed GONUTS page