CAZyme Information: MGYG000002192_00445

Basic Information

• Species: Acutalibacter sp900543305
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Acutalibacter; Acutalibacter sp900543305
• CAZyme ID: MGYG000002192_00445
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
298		33412.46	4.2173

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002192	2487718	MAG	Spain	Europe

• Gene Location: Start: 103218; End: 104114 Strand: -

Full Sequence      

MDSFKKRNLFLAIILVLVVTIVAVSAFLLARGPRESSVELVSRTESGDLLVNDLYDGEMT
IPYYDIPTNSLKLEDFSEKNGVITYDGGDSSVGINVSYKAGTIDWAQVKESGVDFALIRV
GYRGVERGQLVLDKNFEVNITGATEAGLPVGVYFYSKAVTNAEAEEEATFVLEQIREYNI
TYPVAYFWEYDYNDDGSMNQNSRTIQCNGDQVTGFIETFCNKVSSAGYTASYYATKAMGY
ETLDLSKLASYDLWYAEYRTAPSFYYDFEMWQYTQEGTVPGISEKVPVTLALTKYPKK

Enzyme Prediction     

No EC number prediction in MGYG000002192_00445.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	94	282	2.5e-38	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.01e-68	93	286	3	185	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	3.26e-24	93	286	2	181	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.
pfam01183	Glyco_hydro_25	2.26e-18	94	282	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	7.67e-18	93	286	2	179	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.
COG3757	Acm	1.17e-16	93	288	65	250	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQR31703.1	3.42e-111	6	295	4	295
ANU54364.1	3.42e-111	6	295	4	295
ASB42416.1	3.42e-111	6	295	4	295
QNO18615.1	1.39e-75	3	295	10	299
QKN23542.1	9.48e-73	26	295	38	308

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	7.08e-14	94	290	272	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	7.08e-14	94	290	272	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	3.27e-08	117	283	39	193	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.972808	0.024091	0.000984	0.000219	0.000114	0.001810

TMHMM  Annotations     

start	end
7	29