CAZyme Information: MGYG000001260_02364

Basic Information

• Species: Acinetobacter johnsonii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter; Acinetobacter johnsonii
• CAZyme ID: MGYG000001260_02364
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
167		18858.57	10.0195

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001260	3024365	MAG	Italy	Europe

• Gene Location: Start: 1472; End: 1975 Strand: +

Full Sequence      

MSKTKYLAYGLAASAAFFTGLEIHEGYSAKPYKDTGGVVTQGIGSTVKPNGQLIKMTDPH
ITRKTAQEWAKVHVAKDEIPFRKSLQGVKLSQVEYDVYLDFTYNFGQANWNQSSMLRNLK
AGKYKQACDSLLKWKYVAKRDCSVRSNNCYGVWTRQVERHSKCMGAQ

Enzyme Prediction     

No EC number prediction in MGYG000001260_02364.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	14	143	7.7e-30	0.9197080291970803

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16901	lyz_P1	5.17e-52	12	164	1	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.
cd00737	lyz_endolysin_autolysin	8.02e-21	24	136	8	115	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	1.86e-18	11	159	4	138	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	5.23e-18	25	159	19	143	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd00735	T4-like_lys	4.59e-05	21	164	6	139	bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQN40568.1	4.69e-106	2	167	3	168
AYA02219.1	3.86e-105	2	167	3	168
AXY60174.1	3.06e-104	1	167	1	167
QPF36141.1	6.39e-104	2	167	3	168
AZN65181.1	2.60e-103	2	167	3	168

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	4.81e-13	25	134	64	171	ChainA, Lysozyme [Acinetobacter baumannii]
2ANV_A	1.56e-10	19	139	10	128	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]
4ZPU_A	2.41e-07	25	167	35	164	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	2.81e-07	25	167	10	139	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A	4.05e-07	25	167	35	164	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P09963	8.56e-10	19	139	10	128	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 SV=1
P76159	3.83e-08	7	167	5	176	Probable prophage lysozyme OS=Escherichia coli (strain K12) OX=83333 GN=rrrQ PE=3 SV=1
O80292	1.23e-07	25	164	37	163	SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1
P68920	3.72e-07	7	165	17	174	SAR-endolysin OS=Escherichia phage 933W OX=10730 GN=R PE=3 SV=1
P68921	3.72e-07	7	165	17	174	SAR-endolysin OS=Enterobacteria phage VT2-Sa OX=97081 GN=R PE=3 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
0.939590	0.052032	0.007915	0.000142	0.000103	0.000233

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001260_02364.