CAZyme Information: MGYG000001473_01088

Basic Information

• Species: Anaerosalibacter massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Sporanaerobacteraceae; Anaerosalibacter; Anaerosalibacter massiliensis
• CAZyme ID: MGYG000001473_01088
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
233	MGYG000001473_15|CGC1	26353.76	9.1393

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001473	3196506	Isolate	not provided	not provided

• Gene Location: Start: 49274; End: 49975 Strand: -

Full Sequence      

MNLRKLILTENACYKAGRKITPKGIMVHSTGANNPYLRRYVGPDDGQLGVNEYNNHWNQD
RPDGRQVCVHAFIGKLKDGSIATYQTLPWNHRGWHAGGKANDTHIGFEICEDGLTDASYF
NAVYKEAVELCVYLCKLYNLTEKDVIGHYEGYQKGIASNHGDPRNWFPKHGKSMDTFRAD
VKKLLSEGEKPAEQERKKYYRVQIGAYSVKANAEAQLAKAKKAGFTDAFIKYD

Enzyme Prediction     

No EC number prediction in MGYG000001473_01088.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06583	PGRP	1.43e-30	22	166	2	126	Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.
pfam01510	Amidase_2	1.31e-18	21	154	1	116	N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.
smart00644	Ami_2	4.05e-15	21	150	2	119	Ami_2 domain.
COG3023	AmpD	1.39e-06	61	207	60	219	N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis].
pfam05036	SPOR	9.31e-06	197	232	2	37	Sporulation related domain. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOT72278.1	5.87e-130	1	219	1	240
AEY67694.1	1.59e-116	1	214	1	220
CDM67796.1	7.64e-114	1	219	1	240
ABZ85376.1	2.34e-112	1	191	1	191
QAT44066.1	5.62e-112	1	219	1	240

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001473_01088.