CAZyme Information: MGYG000000032_02253

Basic Information

• Species: Hungatella effluvii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii
• CAZyme ID: MGYG000000032_02253
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
519		57441.37	4.9206

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000032	6969476	Isolate	United Kingdom	Europe

• Gene Location: Start: 19135; End: 20694 Strand: -

Full Sequence      

MRYERENRSRKNGRNTRRRWLEDCAAAAAGGIAAVFLFTAMETMGMFPGGDAAVSPVAAE
AQAAAGSQAAVNPAVTESQAAATNPAALQALPASEIRKLAEYQLEAAGKNDRSGTWQETG
VQSRTEKQTVFQTTESDPEHPLIIVDPGHGGTDEGCYAGGVLEKDINLEIAKKLREELVE
SGYRVILTRETDTYMTKEQRAEAANRYGADAFVSIHQNTYEEEEPTGIETYYDGTDPSRD
SRRLALLIHGEAVKRTGAKERELRGDAGFVVTGWTKMPACLIETGFLSSPEEREKLTQAE
YQEKLAEGIAEGIDAFFHPKTMYLTFDDGPSAENTAAVLDVLKARNIKATFFLVGENVRK
NPEVAKRIAAEGHTIGIHCNRHDYEQIYQSTASYLEDFNEAYKTVLKVTGVRVTLFRFPG
GSINAYNKPVYQDIIKEMTARGFIYFDWNASLEDALKKSEPEELIANARETALGRKHVVM
LAHDIVHSTALCLNDLIDQFPEYRMEPLTPEVAPVQFHP

Enzyme Prediction     

No EC number prediction in MGYG000000032_02253.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	318	434	1.1e-26	0.8384615384615385

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10944	CE4_SmPgdA_like	4.98e-69	320	507	1	189	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.
cd02696	MurNAc-LAA	6.65e-69	143	314	2	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.
pfam01520	Amidase_3	3.15e-64	143	313	1	172	N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG0860	AmiC	1.19e-58	124	320	25	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
TIGR02883	spore_cwlD	1.42e-47	143	316	3	189	N-acetylmuramoyl-L-alanine amidase CwlD. Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU23357.1	1.24e-188	141	517	136	512
QRP42504.1	5.03e-188	118	517	102	502
QIB68221.1	2.99e-46	319	518	97	299
QAT41967.1	1.13e-45	319	517	97	298
SDT53150.1	4.31e-45	143	454	59	391

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EMI_A	4.36e-29	142	313	6	174	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A	1.03e-28	143	320	6	185	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5JMU_A	5.13e-28	320	509	20	214	ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
1JWQ_A	1.87e-23	142	320	3	179	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
7RAG_B	1.71e-20	143	316	19	208	ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02114	5.93e-33	143	317	322	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P54525	1.08e-30	139	317	28	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
P50864	1.18e-25	142	320	42	232	Germination-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlD PE=1 SV=1
Q06320	1.69e-22	143	320	4	178	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
O07596	3.91e-22	320	515	85	280	Putative polysaccharide deacetylase YheN OS=Bacillus subtilis (strain 168) OX=224308 GN=yheN 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
0.995391	0.002674	0.000210	0.000063	0.000032	0.001643

TMHMM  Annotations     

start	end
20	42