CAZyme Information: MGYG000002496_00157

Basic Information

• Species: Salmonella bongori
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella; Salmonella bongori
• CAZyme ID: MGYG000002496_00157
• CAZy Family: GH24
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
128		14433.48	6.2091

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002496	4572147	Isolate	Italy	Europe

• Gene Location: Start: 179929; End: 180315 Strand: +

Full Sequence      

MPHISTRFSPACVAFIKQWQGLSLEKYRDRQGNQVIGYGHMLTPDETTTFITPKQAEAFL
LDDLNNCDKLLQTYLPELNDQFQRETLIALMFSIGHQRFLSLINTGDISPTGPGGLSFNL
INSLRLTS

Enzyme Prediction     

No EC number prediction in MGYG000002496_00157.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH24	9	100	7.8e-19	0.6861313868613139

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3772	RrrD	9.92e-30	1	109	1	115	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd00737	lyz_endolysin_autolysin	4.08e-16	12	107	1	102	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.
cd00735	T4-like_lys	3.11e-05	17	109	7	113	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.
cd16900	endolysin_R21-like	2.92e-04	13	108	9	109	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVP37628.1	5.90e-90	1	128	1	128
QXY83490.1	5.90e-90	1	128	1	128
AID26242.1	9.80e-89	1	128	1	128
ASG86296.1	5.03e-69	1	109	1	109
VEA89177.1	8.95e-69	1	116	1	116

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4EVX_A	1.85e-58	5	107	4	106	Crystalstructure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],4EVX_B Crystal structure of putative phage endolysin from S. enterica [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9T1T5	4.47e-10	13	109	8	108	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002496_00157.