CAZyme Information: MGYG000001068_00326

Basic Information

• Species: Streptococcus sp000187445
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus sp000187445
• CAZyme ID: MGYG000001068_00326
• CAZy Family: GH73
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
320		34488.34	7.5021

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001068	2029735	MAG	Sweden	Europe

• Gene Location: Start: 4597; End: 5559 Strand: -

Full Sequence      

MTLDITKTQGTLTIANNDKNRGTFDVVITNLTNPGGITGVVIPVWSDQNGQDDLVWHNAT
KQEDGSYKVTVSASQHKWNSGKYIVHGYLTDASGKNIGFGATSVDVVAPKKIGSASRGNY
DVFNKIVYLDAGHGGYDPGASYFGISEKSLTLAIQSRVKAKLEAEGYQVVTTRTSDTFVD
LTDRSRAANASESDIFVSIHINASGSSAAQGIETYYYQPFAEYPSRINAAYHANPTRLSM
SDTLANAIQSSLINATGAQNQGVKRRTFAVLRETTAPAVLLELGFLSNPQEAARLTTSAY
QETLANAIVAGIKRYYSVYN

Enzyme Prediction     

No EC number prediction in MGYG000001068_00326.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02696	MurNAc-LAA	1.36e-74	126	313	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.
COG0860	AmiC	7.41e-67	98	317	21	229	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520	Amidase_3	1.74e-64	127	312	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.
TIGR02883	spore_cwlD	1.80e-45	125	315	1	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]
pfam08481	GBS_Bsp-like	1.28e-34	14	102	1	89	GBS Bsp-like repeat. This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARI60189.1	1.47e-207	2	316	388	702
QGU82681.1	1.47e-207	2	316	388	702
SQF76003.1	1.47e-207	2	316	388	702
QGU78660.1	1.47e-207	2	316	388	702
QMI50933.1	2.95e-207	1	316	387	702

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JWQ_A	2.18e-32	125	318	2	178	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	6.48e-29	127	315	6	181	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A	4.51e-24	126	315	6	177	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
7RAG_B	3.97e-21	122	318	14	211	ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]
4BIN_A	7.13e-18	126	317	175	394	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54525	3.73e-35	125	316	30	204	Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q02114	2.32e-27	122	316	317	495	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q06320	1.31e-26	127	318	4	177	Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
O48471	1.33e-25	124	312	2	177	Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q8CP02	2.72e-25	125	317	120	290	Probable cell wall amidase LytH OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=lytH 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
1.000059	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001068_00326.