CAZyme Information: MGYG000002317_01566

Basic Information

• Species: Peptoniphilus_A grossensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Peptoniphilus_A; Peptoniphilus_A grossensis
• CAZyme ID: MGYG000002317_01566
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
416		47040.49	9.5449

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002317	2029837	Isolate	France	Europe

• Gene Location: Start: 2420; End: 3670 Strand: -

Full Sequence      

MIKIMLDPGHGGGPAHNRGFKQVDNLPYCNEGDCNFIYARDFLKPALEKYGFKVDMTRSD
IWQNPSLKTRGFMARGYDLLLSVHSNAAGGNVRGVEVWDSTNPKESCKVLGDKICAYVSS
ALGTPNRGTKYRRNNNGSNYYGILRLGYAKKNMIVEHVFHDNLQDATIYRKNLDKTANAV
AKAIAEFYGLAEKTGEVKNPPVELTEEKFIQSIVDSLKGQKLNILPSVTIAQAILESNWG
KSSLAKEACNLFGIKASKDWTGEVYKKQTKEQKPNGEVYTITAVFRKYGSFLESIKDHDK
FFVSTPWRRENYRKVLEAKNYKTQALALRECGYATDLNYGHKLIQLIERLGLQQYDKGVG
KIVTRDNTVPSDWAKEDWEWGKEKGITDGSNPGGVCTREQVISMIRRYDKQREVEK

Enzyme Prediction     

No EC number prediction in MGYG000002317_01566.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH73	219	352	6.6e-34	0.9296875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1705	FlgJ	1.90e-55	200	368	37	200	Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
PRK06347	PRK06347	1.54e-27	92	358	43	305	1,4-beta-N-acetylmuramoylhydrolase.
cd02696	MurNAc-LAA	1.54e-27	3	185	1	172	N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
PRK08581	PRK08581	3.10e-27	174	357	284	473	amidase domain-containing protein.
PRK05684	flgJ	1.73e-26	220	363	168	304	flagellar assembly peptidoglycan hydrolase FlgJ.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDZ74887.1	3.14e-102	1	407	1	411
QHF54940.1	5.71e-45	4	356	719	1081
QXF06253.1	6.06e-45	4	356	852	1222
BBA92865.1	9.88e-43	4	356	719	1081
AUA19299.1	2.22e-38	4	356	861	1232

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FI7_A	3.62e-19	209	356	29	183	CrystalStructure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic domain [Listeria monocytogenes EGD-e]
5DN5_A	5.41e-19	212	350	11	148	Structureof a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5DN5_B Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5DN5_C Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
5DN4_A	7.75e-19	212	350	11	148	Structureof the glycoside hydrolase domain from Salmonella typhimurium FlgJ [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3VWO_A	1.44e-15	219	354	16	150	Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1]
2ZYC_A	1.77e-15	219	354	17	151	ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O32083	3.65e-33	201	375	35	224	Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
P15931	8.36e-18	193	350	139	297	Peptidoglycan hydrolase FlgJ OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=flgJ PE=1 SV=1
P58231	2.73e-17	212	350	157	294	Peptidoglycan hydrolase FlgJ OS=Escherichia coli O157:H7 OX=83334 GN=flgJ PE=3 SV=1
P75942	2.73e-17	212	350	157	294	Peptidoglycan hydrolase FlgJ OS=Escherichia coli (strain K12) OX=83333 GN=flgJ PE=3 SV=1
Q9X9J3	8.87e-14	143	350	100	305	Peptidoglycan hydrolase FlgJ OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=flgJ 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
1.000071	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002317_01566.