CAZyme Information: MGYG000001443_06308

Basic Information

• Species: Streptomyces albus
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Streptomycetales; Streptomycetaceae; Streptomyces; Streptomyces albus
• CAZyme ID: MGYG000001443_06308
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
270		29309.54	11.7171

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001443	7820353	Isolate	not provided	not provided

• Gene Location: Start: 28498; End: 29310 Strand: +

Full Sequence      

MRITSPVRVRRPVTAGAALGAALTVLTALPALAPQAQAAPPSSYRVTGVDTSHHNHGPQE
KTPIDWPRVARGHSFAFFKATQGTRYADPWFARDFAAASRTALVRAPYHFFDPRSAGDGV
AQARHFIATARKAGYQGGRAGELPPVLDIEKVRRGGREMCPPGLRVQQVAAFLKEVRSAF
KAAPIVYTRASFVRECMNGKGNVFAGHPLWLARYGSGAKEPQPVPGAGRSWTFRQYTDKG
RTPGIPGAADLNVFRGSLKELRAMANQRLR

Enzyme Prediction     

No EC number prediction in MGYG000001443_06308.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	49	245	1.6e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	5.09e-50	48	254	2	186	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
cd06524	GH25_YegX-like	1.55e-48	48	256	2	194	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
cd06413	GH25_muramidase_1	5.36e-45	44	256	1	191	Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06412	GH25_CH-type	7.58e-45	46	261	1	199	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
pfam01183	Glyco_hydro_25	1.59e-41	49	245	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QID39861.1	5.23e-165	49	270	1	222
QDY80037.1	6.79e-132	5	268	5	264
QIK11320.1	2.14e-117	49	266	1	218
AWN32268.1	3.04e-117	49	266	1	218
AWK13219.1	2.37e-82	49	265	1	213

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	8.03e-30	46	266	5	214	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.07e-14	44	260	14	212	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
5JIP_A	8.34e-10	64	261	26	229	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	1.56e-28	41	266	62	266	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P25310	1.75e-28	40	266	76	291	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	2.17e-28	41	266	62	266	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	1.16e-27	41	266	62	266	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P26836	8.87e-14	72	262	30	204	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001343	0.993704	0.000537	0.003802	0.000340	0.000242

TMHMM  Annotations     

start	end
13	35