CAZyme Information: MGYG000000015_03409

Basic Information

• Species: Enterobacter mori
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter mori
• CAZyme ID: MGYG000000015_03409
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase AmiB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469		50441.64	9.3504

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000015	4878649	Isolate	United Kingdom	Europe

• Gene Location: Start: 233596; End: 235005 Strand: -

Full Sequence      

MLFPHQAVPYWRDWPVKRRDDGMKNRVKGWLLAATVLLCAQAGAASLSDIQVSNGETQAR
ITFSFMGDPEYAFSQPDSHSVALDIKQTGVIQGLPLRFSGNNLVKSIRSGTPQDSQSLRL
VVDLTEKGKTRAVKQQNGANYTVVFTINADAPPPPPPPAPVVAKRVEEPVYTPRPSEPAR
NPFKSQNDRITAATSSNTVTRPAASARRAAVSGDKVIIAIDAGHGGQDPGAIGPGGTREK
NVTIAVARKLRTLLNDDPMFKGVLTRDGDYFISVMGRSDVARKQNANFLVSIHADAAPNR
SATGASVWVLSNRRANSEMANWLEEHEKQSELLGGAGDVLANSQSDPYLSQAVLDLQFGH
SQRVGYDVATNVLNQLQGIGALHKRRPEHASLGVLRSPDIPSILVETGFISNNGEERLLG
SDSYQQQIAEAIYNGLRKYFEAHPLQSAPQSGAGQTASAALPGEMTATN

Enzyme Prediction     

No EC number prediction in MGYG000000015_03409.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10431	PRK10431	0.0	23	469	1	445	N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860	AmiC	5.39e-77	215	443	42	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696	MurNAc-LAA	1.09e-61	217	436	1	171	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.
PRK10319	PRK10319	5.53e-60	212	451	53	287	N-acetylmuramoyl-L-alanine amidase AmiA.
pfam01520	Amidase_3	2.34e-54	218	436	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCQ47117.1	2.62e-191	23	450	1	420
BCQ41797.1	2.62e-191	23	450	1	420
QZQ49796.1	1.35e-190	23	450	1	418
AUX94894.1	1.03e-189	23	450	1	417
ARJ42298.1	1.10e-188	23	450	1	418

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BIN_A	6.62e-47	70	440	48	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A	7.88e-29	218	441	7	225	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A	5.87e-25	215	441	4	179	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A	1.89e-17	217	441	3	177	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
7RAG_B	2.67e-16	214	448	16	217	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
P26366	7.56e-256	23	469	1	439	N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P26365	2.11e-245	23	469	1	445	N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P44493	3.23e-81	216	436	23	243	Probable N-acetylmuramoyl-L-alanine amidase AmiB OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=amiB PE=3 SV=1
P57638	2.29e-55	215	440	4	228	Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
Q8K908	1.12e-49	220	441	2	223	Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) OX=198804 GN=amiB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.288284	0.687588	0.022474	0.000696	0.000414	0.000536

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000015_03409.