CAZyme Information: MGYG000001164_00470

Basic Information

• Species: Prevotella lascolaii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella lascolaii
• CAZyme ID: MGYG000001164_00470
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
161		18606.08	10.94

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001164	3302780	MAG	Austria	Europe

• Gene Location: Start: 16312; End: 16797 Strand: +

Full Sequence      

MRLMILLALLLVSGSLSAQTQGAIKRVRHVSRFELAVACIKKYEGLHGPKHHPYVGYGHK
LLPGEKFSPRMTERQADALLRSDLRKLCAMFRDFGRDSLLLATLAYNVGCGKVMKSRMYA
KMRSGNRNIYRDYVDFKRWNGKIVPSIERRRKMEYLLLFTP

Enzyme Prediction     

No EC number prediction in MGYG000001164_00470.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	36	154	4.3e-16	0.9635036496350365

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	4.80e-20	40	157	5	134	endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16901	lyz_P1	1.16e-10	49	157	24	138	P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16900	endolysin_R21-like	4.20e-09	36	157	8	140	endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772	RrrD	3.45e-08	33	154	8	143	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT58718.1	6.31e-110	1	161	1	161
AZS30124.1	1.10e-52	32	159	35	169
QUT99619.1	1.10e-52	32	159	35	169
QUT67552.1	1.10e-52	32	159	35	169
QUT63230.1	2.29e-52	31	159	37	170

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000254	0.999180	0.000155	0.000136	0.000130	0.000135

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001164_00470.