CAZyme Information: MGYG000000111_02340

Basic Information

• Species: Cutibacterium acnes
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium acnes
• CAZyme ID: MGYG000000111_02340
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
277	MGYG000000111_6|CGC1	30180.92	4.47

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000111	2484103	Isolate	Canada	North America

• Gene Location: Start: 13551; End: 14384 Strand: +

Full Sequence      

MVSGMTVITLVPAAVAHASETQLPEESSSSSAPSSSDHAMGSQIKKHEHETAVTNRVQSL
TIDTEPEGMDVSSHDGNVDWPAKVSSGMSFAWVKATEGTSYQNPFYASQYNGSQSAGLIR
GAYHFALPSNSSGQAQATYFSDHGGGWSEDGYTLPGVVDLEYNPYGENACYGLSQTAMAS
WIRDFVSTYQERWGRAPMIYTSTSWWNMCVGSAASDITAVAPLWIARYSSTVGELPSGWD
AWTMWQYSDTGYDHDRMAGTREDLEKFATNETATPRH

Enzyme Prediction     

No EC number prediction in MGYG000000111_02340.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	69	252	3.9e-53	0.9717514124293786

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06412	GH25_CH-type	2.50e-115	66	264	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	1.32e-58	70	252	2	176	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	2.91e-53	68	252	2	173	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	5.15e-37	68	251	2	178	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.
cd06525	GH25_Lyc-like	2.14e-30	68	252	2	171	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAZ51538.1	7.57e-207	1	277	1	277
AXM07712.1	7.57e-207	1	277	1	277
ALT35754.1	7.57e-207	1	277	1	277
ALU23845.1	7.57e-207	1	277	1	277
AEH29982.1	7.57e-207	1	277	1	277

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	3.09e-66	67	273	6	206	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
6ZM8_A	1.87e-65	68	271	4	208	ChainA, muramidase [Sodiomyces alcalophilus]
6ZMV_A	2.35e-63	68	268	4	204	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A	8.36e-62	64	269	2	209	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]
4KRU_A	1.56e-16	67	251	21	193	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.80e-64	67	273	83	283	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P00721	1.78e-55	67	269	3	210	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
D4ANU4	2.35e-53	67	268	31	232	N,O-diacetylmuramidase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05911 PE=1 SV=1
P26836	2.44e-15	67	251	10	182	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8FFY2	7.23e-14	68	275	69	272	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX 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
0.015946	0.982939	0.000283	0.000317	0.000249	0.000228

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000111_02340.