CAZyme Information: MGYG000002148_02828

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella
• CAZyme ID: MGYG000002148_02828
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
471		50795.67	4.8376

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002148	4597814	MAG	United States	North America

• Gene Location: Start: 39376; End: 40791 Strand: -

Full Sequence      

MKVRKRVISLLLAAFVAVGSFLAAPVKAEAAAPLAKGIDVAKYQGAVNWSAVKKAGYDFA
FIKIGSAKSGLDPYYAANMAGANAAGLKVGAYIYSYATTVEGAITEAQFAIAALEPYTVS
FPVVYDLEDSVHKNMTPDQLAALTVAFCTTVQSAGYYPMVYSSKNWMVGKIAATPFDKWI
AQYNSVCEYPNPAFWQFTSSGSVPGIDGRVDLNYQFKDYSNLIVANGFVDRGGSRYYYKN
YRMQFGFVEDGGKRYFMNADGTMYKQGWLGDGVNMFYMDTKDGHMLTDLVEIGGKKYYFA
ASGLMQRGMIPLDGKIYLFGADGAMQHGFYTDPAAGIRYFKEDGSMASNELLTVNGNKYY
FNPGGIMVTGMAPVGGLTYLFGADGAMQYGWYTDASGMRYFQADGSMAVNTTLTVDGVMY
TFDANGIAAAVPVLNPTAWVTDPETGVTVDTSTGETVDPAVVAEVTAALAQ

Enzyme Prediction     

No EC number prediction in MGYG000002148_02828.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	38	206	4.3e-45	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.07e-64	36	216	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	9.38e-34	36	214	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	7.24e-27	38	206	1	180	Glycosyl hydrolases family 25.
NF033930	pneumo_PspA	2.89e-26	225	426	462	657	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033838	PspC_subgroup_1	1.34e-23	246	426	487	680	pneumococcal surface protein PspC, choline-binding form. The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL32940.1	2.24e-67	34	304	39	310
AOZ95227.1	9.20e-62	2	312	3	319
CBK77005.1	3.31e-53	35	285	51	301
QQR03194.1	5.57e-50	34	237	99	303
ANU47907.1	5.57e-50	34	237	99	303

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.72e-13	36	213	17	204	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2WW5_A	5.42e-12	36	213	270	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	1.27e-11	36	213	270	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	2.08e-11	36	213	6	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	5.96e-08	36	213	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	2.91e-10	36	213	83	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	9.72e-07	36	228	10	207	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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
0.000233	0.999123	0.000152	0.000190	0.000156	0.000140

TMHMM  Annotations     

start	end
7	26