CAZyme Information: MGYG000002513_02886

Basic Information

• Species: Morganella morganii_A
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Morganella; Morganella morganii_A
• CAZyme ID: MGYG000002513_02886
• CAZy Family: GH24
• CAZyme Description: Lysozyme RrrD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
158	MGYG000002513_237|CGC1	17047.5	9.1047

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002513	3981937	Isolate	United States	North America

• Gene Location: Start: 955; End: 1431 Strand: -

Full Sequence      

MNNNLSKKAAAAAAGGAVAAALVLITAYEGVEYKPYRDVAGVLTVCYGHTGGDIQTGKIY
TADECRALLHRDLEKVRRAVDPMIKVPVDDTTRAAIYSFVYNTGPGAFSRSAMLRKLNAG
DIAGACDEMKRWTFAGGKQWQGLINRRETESTVCRATL

Enzyme Prediction     

No EC number prediction in MGYG000002513_02886.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	20	150	5.9e-47	0.9708029197080292

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16900	endolysin_R21-like	5.01e-73	25	155	12	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	4.65e-50	25	150	5	131	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	6.21e-44	28	155	18	148	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	3.97e-32	25	154	10	139	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	1.03e-25	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
QXO71576.1	1.01e-100	1	158	1	158
QXO64152.1	8.29e-100	1	158	1	158
QXO79232.1	8.29e-100	1	158	1	158
QXO48660.1	8.29e-100	1	158	1	158
QXO56440.1	8.29e-100	1	158	1	158

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZPU_A	2.15e-56	29	154	35	160	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]
3HDF_A	8.22e-56	29	154	10	135	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	1.81e-55	29	154	35	160	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]
6ET6_A	1.66e-25	24	150	59	189	ChainA, Lysozyme [Acinetobacter baumannii]
2ANV_A	1.21e-16	29	150	16	140	ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O80292	1.19e-58	29	154	37	162	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
O80288	2.77e-57	29	154	37	162	SAR-endolysin OS=Bacteriophage PS34 OX=83127 GN=19 PE=3 SV=1
P78285	8.59e-56	29	154	35	160	Lysozyme RrrD OS=Escherichia coli (strain K12) OX=83333 GN=rrrD PE=1 SV=1
P10439	4.94e-55	29	154	35	160	SAR-endolysin OS=Enterobacteria phage PA-2 OX=10738 GN=15 PE=3 SV=1
P27359	2.31e-53	29	154	35	160	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
0.887669	0.111318	0.000496	0.000213	0.000124	0.000180

TMHMM  Annotations     

start	end
9	31