CAZyme Information: MGYG000000123_02824

Basic Information

• Species: Blautia sp001304935
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp001304935
• CAZyme ID: MGYG000000123_02824
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
405	MGYG000000123_8|CGC4	44341.49	4.1889

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000123	5803260	Isolate	Canada	North America

• Gene Location: Start: 161419; End: 162636 Strand: +

Full Sequence      

MNMIRRVSSYILFFGVFMLLGCTSVFALPPEDGNQRQGIDVSMWQGDIDFEEVAGTGVDT
VYIRSSLGSDYTDPYFEHNYERARAAGLNVGFYHYVTARTVSQAVYEAHFYVNVIQGKEF
QCRLAMDFEDLTRLSAGEANEIGLAFIRTVENLSGKGTVVYSDAYNAGNVFGGELTEYPL
WIAEYDVSEPSSQVNWDSWAGWQYSDTGNVAGISGYVDLDRYTDAMFLEEAGSVPGPVPM
PEPSSSTVEYTVKSGDTLWGIARMYRTSVSAIVSENGIANPNLIYPGEVLRITLADQVSS
SQVDNTYMVRRGDTLWGIARMYRISVARLAAINHISDPNLIYPGEVLQISASGSTGDVGR
TYIVRYGDTLSGIADRFGTTVSQLAAVNGIADPNLIYAGEVLTVS

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	39	213	2.7e-47	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	7.57e-72	37	222	1	184	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.
cd00599	GH25_muramidase	1.65e-48	37	222	1	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.
pfam01183	Glyco_hydro_25	5.38e-45	39	213	1	180	Glycosyl hydrolases family 25.
cd06414	GH25_LytC-like	1.89e-42	36	220	1	188	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.
cd06524	GH25_YegX-like	1.05e-38	38	222	2	192	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBE96304.1	4.00e-250	3	405	1	403
QIB56830.1	8.07e-250	3	405	1	403
QMW80393.1	8.07e-250	3	405	1	403
ANU77129.1	9.52e-242	3	405	1	403
QJU17248.1	9.52e-242	3	405	1	403

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.78e-43	37	231	21	216	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	8.78e-42	37	231	21	216	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A	1.97e-24	28	224	14	203	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	1.30e-18	32	222	1	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4B8V_A	3.80e-15	244	400	38	212	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.93e-41	28	224	1	198	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	9.08e-28	37	228	2	186	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P76421	7.14e-24	6	222	41	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	9.83e-24	6	222	41	254	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	9.83e-24	6	222	41	254	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000810	0.246593	0.752036	0.000210	0.000202	0.000152

TMHMM  Annotations     

start	end
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