CAZyme Information: MGYG000002945_03642

Basic Information

• Species: Bariatricus massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Bariatricus; Bariatricus massiliensis
• CAZyme ID: MGYG000002945_03642
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
320		35417.62	6.469

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002945	3969748	MAG	United States	North America

• Gene Location: Start: 4455; End: 5417 Strand: +

Full Sequence      

MSLNGIDISEYQSGIDLRLVPCDFVICKATQGTSYVNPDCDRAYQQAKGLGKKLGVYHYF
SGGNPVSEAQYFVNNIKGYIGEALLALDWEQNENVSFGQGAAVAVQFLNEVFRLTGVRPL
IYMSKSTCRNYNWSSVVNGNYGLWMAQYANNDPTGYQSNPWTDNLGIGAFKFYAIHQYSS
TGRLAGYDGNLDLDIFYGDRGAWDAYAKGRRTENETEPSTPEAVTYIVKRGDTLSGIAAM
FGTTYQQLAAENGITNPNLIYPGQVLRIRGGSQPLYYTVKRGDTLSEIAARYGTTYQQLA
QLNGITNPNLIYAGQVIRIR

Enzyme Prediction     

No EC number prediction in MGYG000002945_03642.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	186	1.4e-42	0.9887005649717514
CBM50	277	319	6.3e-17	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	9.39e-89	3	203	1	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd06525	GH25_Lyc-like	1.23e-45	4	196	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	9.82e-40	5	196	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	7.70e-39	6	186	1	179	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	1.00e-29	5	198	2	194	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
CBK80688.1	1.45e-111	1	320	1	362
QCT71511.1	3.81e-103	3	319	2	325
QCT70818.1	1.63e-99	3	319	2	325
QOP65129.1	3.37e-97	1	320	1	340
QHJ76374.1	1.30e-89	3	319	1	326

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	6.83e-20	2	196	19	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	4.12e-19	2	196	19	207	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]
2WAG_A	2.15e-08	3	206	16	216	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
5JCD_A	2.90e-08	226	319	85	191	Crystalstructure of OsCEBiP [Oryza sativa Japonica Group],5JCD_B Crystal structure of OsCEBiP [Oryza sativa Japonica Group],5JCD_C Crystal structure of OsCEBiP [Oryza sativa Japonica Group]
5JCE_A	7.05e-08	226	319	85	191	Crystalstructure of OsCEBiP complex [Oryza sativa Japonica Group],5JCE_B Crystal structure of OsCEBiP complex [Oryza sativa Japonica Group]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q49UX4	6.77e-24	225	319	87	193	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q8CMN2	2.91e-21	219	319	79	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	2.91e-21	219	319	79	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q7A7E0	2.53e-18	212	319	77	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain N315) OX=158879 GN=sle1 PE=1 SV=1
Q2FJH7	2.53e-18	212	319	77	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sle1 PE=3 SV=1

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
1.000076	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002945_03642.