CAZyme Information: MGYG000002945_00521

Basic Information

• Species: Bariatricus massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Bariatricus; Bariatricus massiliensis
• CAZyme ID: MGYG000002945_00521
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
291	MGYG000002945_2|CGC1	33337.19	4.0228

Genome Property

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

• Gene Location: Start: 135595; End: 136470 Strand: +

Full Sequence      

MKKYTALFLMLTLMLAGCTGCEKSEKVPAPETEEKKEDVEETETYTFVDVLGESYVAELR
EDVPACTYDYEYLTWENGYPYYKDEDGKVLSELGVDVSKYQEAVDWNQVREAGMSFAIVR
LGFRGYGEEGKLVLDEYYEQNVQAAAAAGLKVGVYFFSQAVTEEEAREEAQFVLEHTAGY
TIEGPIVFDTEEIKDDTARTDNLTREEITRHCIAFCEAVEEAGREPMIYANMKWMAFTLE
LEKLTKYDKWYADYEAAPQCPYEFTIWQYTESGTVPGIQGNADINVWFHTL

Enzyme Prediction     

No EC number prediction in MGYG000002945_00521.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	95	278	8.3e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.80e-86	94	288	3	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	5.10e-36	94	287	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.
cd06413	GH25_muramidase_1	7.55e-32	94	289	5	190	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.
cd06525	GH25_Lyc-like	9.49e-30	94	285	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.
pfam01183	Glyco_hydro_25	6.55e-29	95	278	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEK18217.1	1.12e-113	6	288	17	298
QYX28904.1	4.59e-113	7	288	10	285
QRO38911.1	2.07e-111	5	291	9	288
QBF76167.1	2.07e-111	5	291	9	288
BBF45127.1	1.06e-106	20	288	5	277

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	3.47e-13	94	288	18	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
5A6S_A	6.98e-12	90	285	14	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WW5_A	3.32e-10	95	288	272	468	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	7.99e-10	95	288	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	1.70e-08	94	285	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	1.71e-11	94	291	69	258	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	2.33e-11	94	291	69	258	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	2.33e-11	94	286	69	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P34020	1.35e-08	94	285	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
P25310	1.69e-07	94	285	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm 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
0.000000	0.000010	1.000021	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002945_00521.