CAZyme Information: MGYG000001497_01231

Basic Information

• Species: Clostridium_F niameyense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_F; Clostridium_F niameyense
• CAZyme ID: MGYG000001497_01231
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
283	MGYG000001497_6|CGC9	32381.71	8.6216

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001497	2542824	Isolate	not provided	not provided

• Gene Location: Start: 1055759; End: 1056610 Strand: +

Full Sequence      

MESNGKDNIRGIDISSWQTGINYRKVKEFGDVVIIKATEGVDYVDSMLEKHYEGAKSAGL
KVGFYHFFSDKTNPIEQAKDFWNAIKNKKFEVIPVLDIETSKRSKKEVTDRCILFLNEMK
RLSGFDCIIYTYTNFARTKLDTRLSKYLLWIAEYGVNWPGSNGIWTSWVGFQYTDKAKVP
GVPNLCDANKFTEGIYINGGRKKVKYIVIYNNGADQRAAEYLADFLSCPTISNSRAFDYS
TVEHVYAVGYTKEHYTSYVEKVISGDGRYSTLEAVLKYIRENS

Enzyme Prediction     

No EC number prediction in MGYG000001497_01231.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	12	182	7.2e-50	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	1.48e-89	10	191	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	2.02e-55	10	191	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	6.13e-51	12	182	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	3.84e-43	2	195	56	257	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06524	GH25_YegX-like	1.42e-42	10	191	1	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
AEB76049.1	8.30e-102	1	197	1	197
AYF54873.1	6.51e-101	1	197	1	197
QPW61801.1	6.73e-101	1	197	1	197
QPW58887.1	6.73e-101	1	197	1	197
QPW56281.1	1.31e-100	1	197	1	197

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.89e-58	8	198	19	214	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A	3.24e-58	13	280	26	291	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4KRT_A	6.40e-57	8	198	19	214	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]
4CU2_A	1.76e-27	207	280	4	77	C-terminaldomain of CTP1L endolysin mutant V195P that reduces autoproteolysis [Clostridium phage phiCTP1]
5A6S_B	1.76e-27	207	280	4	77	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	9.36e-57	1	195	1	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.16e-36	9	199	1	188	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	3.21e-20	9	191	67	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	3.21e-20	9	191	67	254	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	1.18e-19	9	191	67	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001497_01231.