CAZyme Information: MGYG000000545_00221

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter
• CAZyme ID: MGYG000000545_00221
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
315		36394.4	4.0502

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000545	2021811	MAG	Fiji	Oceania

• Gene Location: Start: 104808; End: 105755 Strand: +

Full Sequence      

MKDQINGEDRVKNRIRKTVLLLSVMMLFTGCAANSGKTVETTADDVENSESGVVTEQENG
KTYFVFQDVKEEEYRAELLDDVPENTYNFKNLSMDEETGYKSYYDEKNQVSAKKGIDVSE
FQGEEIDWKQVKESGIDFVILRLGYRAYGETGQLVLDDMFAQNAEGAIEAGLDVGVYFFS
QAISPAEAVEEADFVLEHIQPYKIRGPVVYDTEEIKDDTARTDDNTREEFTNYCKIFCDG
IRQAGYDPMIYANMKWMAFTLKMEELTEYDFWYADYHEVPQCPYQYKMWQYSETGEVPGI
KGNVDLDLWFQEEVR

Enzyme Prediction     

No EC number prediction in MGYG000000545_00221.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	116	300	5.3e-45	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.47e-92	113	310	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	5.43e-37	114	309	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	1.99e-27	116	300	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.19e-27	114	307	1	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	9.92e-26	114	306	4	186	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	1.37e-157	20	313	10	305
QRO38911.1	2.56e-101	11	311	2	286
QBF76167.1	2.56e-101	11	311	2	286
QYX28904.1	3.75e-101	11	310	2	285
QEK18217.1	1.20e-94	12	311	10	299

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.75e-13	114	312	21	210	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.19e-12	114	312	21	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]
1JFX_A	7.44e-07	110	305	2	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	5.35e-06	113	315	22	207	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	1.21e-10	114	314	10	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8FFY2	1.13e-09	115	309	69	254	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.52e-09	115	309	69	254	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.52e-09	115	309	69	254	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P34020	1.59e-09	114	307	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

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
0.000968	0.006861	0.992076	0.000134	0.000029	0.000011

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000545_00221.