CAZyme Information: MGYG000004797_02106

Basic Information

• Species: Phocaeicola sartorii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sartorii
• CAZyme ID: MGYG000004797_02106
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
172		19197.41	9.0961

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004797	5247182	MAG	China	Asia

• Gene Location: Start: 27077; End: 27595 Strand: -

Full Sequence      

MRVITTAIYLILTCCGMVVQAQGGGSSPPAAEQIPDSLFNKAVACIKGHEGWHGNHLPYV
GYGHKLLPGETFTPDMSEAQADSLLKADLMKLCRMCGRFGKDALLVATLSYNVGYYRLVG
YGKIPKSRLVQKLEAGDRDIYDEYISFRCYKGKVIPSIERRRKKEFNLLYIP

Enzyme Prediction     

No EC number prediction in MGYG000004797_02106.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	2.19e-13	46	168	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.
cd16900	endolysin_R21-like	2.20e-05	42	165	8	137	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.
cd16901	lyz_P1	4.09e-04	56	168	26	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT82153.1	2.53e-128	1	172	1	172
QQR16310.1	1.66e-99	1	170	1	170
QUT63230.1	9.62e-99	1	170	1	170
ANU58767.2	2.08e-96	10	170	3	163
QJR76753.1	3.59e-86	16	170	18	165

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
0.000191	0.999186	0.000156	0.000144	0.000131	0.000126

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004797_02106.