CAZyme Information: MGYG000000337_01793

Basic Information

• Species: Morganella morganii_B
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Morganella; Morganella morganii_B
• CAZyme ID: MGYG000000337_01793
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
338		35740.36	9.9637

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000337	3835549	MAG	Sweden	Europe

• Gene Location: Start: 11758; End: 12774 Strand: -

Full Sequence      

MVRESRAPDAQHQRIVLELADKNSFRDAADNSGLIITLIGKNSYTSAPVAAAQPVTTTTD
KPLRMNSGSAAPAAPVATTPAAAPAQAKIPVVPTGKLPKNSRQVVVAIDAGHGGKDPGAI
GQNGLKEKNVTISIARKLEKRLKDDPMFKPVLTRDGDYFISVAGRSEVARKFGSNMLVSI
HADSAPNRTATGSSVWVLSNRRANNELGNWLEQSEKQSELLGGAGDALANGADPYLSQAV
LDLQFGNSQRVGYAVAQDVIRQLRKIGKVHKGTPEHASLGVLRSPDIPSILVETGFISNS
TEEQLLGSDTYQEQVAAAIHGGLRAYFTANPLQAAPSK

Enzyme Prediction     

No EC number prediction in MGYG000000337_01793.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10431	PRK10431	1.76e-149	2	336	85	425	N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860	AmiC	1.40e-73	89	330	28	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696	MurNAc-LAA	2.15e-59	105	323	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	2.38e-55	98	338	52	287	N-acetylmuramoyl-L-alanine amidase AmiA.
pfam01520	Amidase_3	2.64e-53	106	323	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
AYW95163.1	1.54e-128	2	336	82	430
AYX15905.1	1.54e-128	2	336	82	430
AYX00377.1	1.54e-128	2	336	82	430
ABS48255.1	1.54e-128	2	336	82	430
AYW89628.1	1.54e-128	2	336	82	430

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BIN_A	8.33e-46	88	327	155	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A	2.66e-31	106	326	7	223	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A	6.13e-23	101	326	2	177	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A	3.01e-20	105	326	3	175	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A	4.19e-16	101	326	1	181	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26365	5.09e-117	103	336	191	425	N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P26366	1.36e-115	103	336	185	419	N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P44493	7.33e-86	104	326	23	246	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	1.02e-56	101	328	2	229	Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
Q8K908	1.48e-48	108	327	2	222	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000046	0.000016	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000337_01793.