CAZyme Information: MGYG000000102_00273

Basic Information

• Species: Terrisporobacter sp902363255
• Lineage: Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Terrisporobacter; Terrisporobacter sp902363255
• CAZyme ID: MGYG000000102_00273
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
431	MGYG000000102_1|CGC2	47825.21	9.3074

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000102	3838773	Isolate	Canada	North America

• Gene Location: Start: 278915; End: 280210 Strand: -

Full Sequence      

MIKRDKSLLAMSLGIVISSQGMTTISDADSLSTNIDNYQAQRSGNQSDPMQNNNHNMGGN
SSRIYTVGDDVFNSNKVTLSNPNAIGSGTVTESYLNVRSIPSTSSQLVGTLAYNERVDIL
EKSNGWYKIDFRGTQGYVASSYLKLNPIEKGIDVSKWNGNIDWNKVKNSGVDYVIIRGGF
GTSTVDSKFKTYIEGASNAGLKVGVYWFSYATTPEKAVQEARKCLQTISPYRNSITYPVF
FDYEYDSVKYANSNDVLITKNSATQIANSFINTIKAYGYDTGIYTNKNFSSTYFTDELIN
STNLWVAQYNTTNTFNNTYSMWQYSEKGVVPGISSYVDLNYTYLRTPKNNIRTYSNSSVQ
TQSSAGNLSATKKGVTTVNLNLRKDLSASPSIINTIPANTTIEVLEQLSSGWYKVKYKHF
VGYVAGNYVNM

Enzyme Prediction     

No EC number prediction in MGYG000000102_00273.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	152	333	6e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.94e-76	150	343	2	191	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	1.22e-42	150	341	1	185	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	8.03e-36	152	333	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.14e-35	150	341	1	183	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	3.76e-31	150	358	64	269	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
QRI51984.1	1.53e-44	150	347	3	197
AJD26091.1	5.83e-44	150	347	3	197
QJD46409.1	5.83e-44	150	347	3	197
AXG95866.1	5.83e-44	150	347	3	197
QMU01264.1	5.83e-44	150	347	3	197

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRT_A	5.13e-20	150	429	21	283	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]
4KRU_A	3.16e-13	150	340	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A	6.11e-11	148	341	21	200	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	2.04e-10	150	340	6	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2KYB_A	3.56e-09	93	143	10	60	Solutionstructure of CpR82G from Clostridium perfringens. North East Structural Genomics Consortium Target CpR82g [Clostridium perfringens ATCC 13124]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.28e-17	150	429	10	272	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.05e-14	150	340	2	178	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
P25310	2.61e-09	150	340	83	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
0.000447	0.997811	0.001116	0.000231	0.000204	0.000167

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000102_00273.