CAZyme Information: MGYG000003984_00836

Basic Information

• Species: Mediterraneibacter sp900752395
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900752395
• CAZyme ID: MGYG000003984_00836
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
335		38308.87	4.4623

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003984	2095190	MAG	United Kingdom	Europe

• Gene Location: Start: 26321; End: 27328 Strand: -

Full Sequence      

MGRGGNKVNGKENANDRRKKHFKGSVGKCLLLIGCLLLLTACSSKKETFSPNVTEEPKEE
TVKDWIAQSNGSFLKNADGNSEEKLYCFQDVEGNSYEASLLETVPKCSYDFSYLKNDEKT
GYKRYEDPKGNVTARFGIDVSEFQGEEIDWKQVKESGIEFVMIRLGYRAYGESGSLVLDA
MYDQNVKGALEAGLQVGVYFFSQAVSPVEAVEEAEFVLEHLKHYEITGPVVFDTEEIKWD
TARTDDNTRQDFTNYCKVFCDTIKHAGYDPMIYANMKWMTFMLDMEQLGEYDFWYADYHE
IPQCPYHYKIWQYSETGAVPGIAGNVDLNLWFQED

Enzyme Prediction     

No EC number prediction in MGYG000003984_00836.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	138	322	2.3e-45	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.77e-94	135	332	1	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	5.20e-38	137	331	2	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	1.04e-30	138	322	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.72e-28	137	329	2	182	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.
cd06413	GH25_muramidase_1	4.34e-26	137	329	5	187	Uncharacterized bacterial muramidase containing 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
CBL26148.1	6.42e-140	18	335	2	305
QEK18217.1	3.06e-105	69	335	37	301
QRO38911.1	2.60e-101	77	333	35	286
QBF76167.1	2.60e-101	77	333	35	286
QYX28904.1	2.69e-101	77	332	35	285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	5.08e-17	137	334	22	210	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.40e-16	137	334	22	210	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]
3HMC_A	4.61e-07	138	329	8	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
1JFX_A	8.27e-07	137	329	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	2.52e-06	128	329	16	199	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	1.86e-14	137	334	11	199	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	3.19e-10	137	329	3	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
Q8X7H0	7.20e-10	99	331	22	254	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	9.72e-10	99	331	22	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	9.72e-10	137	331	69	254	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.004893	0.368080	0.626747	0.000222	0.000055	0.000016

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003984_00836.