STRGL:LYSM1

Species (Taxon ID)	Streptomyces globisporus. (1908)
Gene Name(s)	acm
Protein Name(s)	Lysozyme M1 1,4-beta-N-acetylmuramidase M1
External Links
UniProt	P25310
EMBL	M30645
PIR	JQ0529
PDB	1JFX
PDBsum	1JFX
ProteinModelPortal	P25310
SMR	P25310
CAZy	GH25
PRIDE	P25310
EvolutionaryTrace	P25310
GO	GO:0005615 GO:0003796 GO:0005975 GO:0016998 GO:0009253
Gene3D	3.20.20.80
InterPro	IPR002053 IPR008270 IPR013781 IPR018077 IPR017853
Pfam	PF01183
SMART	SM00641
SUPFAM	SSF51445
PROSITE	PS00953

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	0008152	metabolic process	PMID:11427528	ECO:0000314			P		The metabolic process has to do with the structure of the overall protein. The structure of Cellosyl comprised to a single domain,is demonstrated in figure 2. Where it is shown that the structure is comprised of eight beta strands and six alpha helices. Shown with the strands forming the staves of the barrel and the helices located around it. Helices are depicted in red, loops in green, the parallel βeta-strands in blue, and the antiparallel βeta-strand is highlighted in yellow.	complete CACAO 12878
	GO:0003796	lysozyme activity	PMID:11427528	ECO:0000314			F		Figure 1 displays that unlike other lysozymes (HEWL, GEWL, and T4L-types), the Ch-type lysozymes have both Beta-1,4-N-acetyl- and Beta-1,4,-N,6-O-diacetylmuramidase activities. Due to this characteristic they are able to cleave the 6-O-acetylated peptidoglycans. This icnludes the peptiodglycans that are present in cell walls of Staphylococcus aureus. Figure 2 displays that the structure of Cellosyl contributes to its function. Figure two shows that Cellosyl comprises a single domain. The enzyme is shown to have a beta/alpha-barrel fold. This is different than many other enzymes which have (Beta/alpha)8-barrels. All of these specific folds allow for the active site to be locate at the C-terminal end of the beta-barrel. Figure 3 compares the amino acid sequence of various Ch-type lysozymes and it supports that the active site is located at the C-terminal end of the Beta-barrel. It does so because it shows that the amino acids at the C-terminal ends of Beta1 and Beta4 are highly conserved among lysozymes from bacteria and Chalaropsis. Figure 4 displays how the charges are distributed on the surface of Cellosyl and how that impacts it's lysozyme activity. Due to the grove in the substrate-binding site, there is a high negative electrostatic potential. This is developed to the deep hole.	complete CACAO 12908
Contributes to	GO:0003796	lysozyme activity	PMID:11427528	ECO:0000255		UniProtKB:P25310	F		Figure 1 shows four different classes of endo-N-acetylmuramidases which all use lysosome structures and this is presented in the cellosyl. This shows that lysozyme activity is being used.	complete CACAO 12911
enables	GO:0003796	lysozyme activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002053 InterPro:IPR008270	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 InterPro:IPR008270	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 InterPro:IPR008270	P		Seeded From UniProt	complete
enables	GO:0003796	lysozyme activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.17	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	P		Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0112	C		Seeded From UniProt	complete
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References

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