CAZyme Information: MGYG000004295_02752

Basic Information

• Species: Providencia rettgeri
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rettgeri
• CAZyme ID: MGYG000004295_02752
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
189	MGYG000004295_76|CGC1	20712.2	9.1728

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004295	4142275	MAG	Israel	Asia

• Gene Location: Start: 15212; End: 15781 Strand: -

Full Sequence      

MAKIPNKIKMAAAAGGLVTLTVAMIAEFEGYESKPYRDVVGVLTVCYGHTGPDIIPTKTY
TKAECYALLEKDLAIVAKAVNPLIKVNIPDYTRAALYSFTYNVGTGAFSRSTLLKKLNAG
DQAGACNELKRWIYAGGVKWKGLMTRREVEKAVCLGEFAYAYPLSLSDSLSTWQLAYMYS
EMIPAVLTR

Enzyme Prediction     

No EC number prediction in MGYG000004295_02752.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	22	150	1.6e-47	0.9562043795620438

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16900	endolysin_R21-like	3.61e-81	14	155	1	142	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.
cd00737	lyz_endolysin_autolysin	9.41e-59	22	155	2	136	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.
COG3772	RrrD	2.83e-55	22	156	12	149	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	1.26e-45	21	155	6	140	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.
pfam00959	Phage_lysozyme	2.04e-30	42	148	1	107	Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKG44818.1	3.36e-130	1	189	1	189
QNN34951.1	3.36e-130	1	189	1	189
QNP21085.1	1.60e-128	1	189	1	189
BBV04195.1	1.26e-125	1	189	1	189
QIF60556.1	1.25e-123	1	189	1	190

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZPU_A	5.47e-60	6	155	6	161	Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]
3HDE_A	4.59e-59	6	155	6	161	ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
3HDF_A	1.18e-58	29	155	10	136	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
6ET6_A	2.39e-24	6	155	39	194	ChainA, Lysozyme [Acinetobacter baumannii]
7M5I_A	1.12e-13	25	155	17	154	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O80292	2.62e-63	10	155	12	163	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288	2.47e-61	10	155	12	163	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
P78285	2.18e-59	6	155	6	161	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1
P10439	1.25e-58	6	155	6	161	SAR-endolysin OS=Enterobacteria phage PA-2 OX=10738 GN=15 PE=3 SV=1
P27359	2.90e-57	6	155	6	161	SAR-endolysin OS=Enterobacteria phage P21 OX=10711 GN=R PE=1 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
0.979341	0.020420	0.000124	0.000051	0.000025	0.000051

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004295_02752.