CAZyme Information: MGYG000001457_01071

Basic Information

• Species: Pseudomonas_B luteola
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_B; Pseudomonas_B luteola
• CAZyme ID: MGYG000001457_01071
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase AmiC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
403	MGYG000001457_1|CGC9	43791.33	10.4581

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001457	5659210	Isolate	not provided	not provided

• Gene Location: Start: 1043203; End: 1044414 Strand: -

Full Sequence      

MNRRRLLNLLLASLTLPAAFPVLALPQRLTSARAWLDSDKFRLVFDLSGPVRFKTFRLSA
PDRIILDLANTQQVAALNNVPLKNTPVRSIRSAPFGSSDTRVVLELSQPVTLDSFLLGPA
ENAGHRLVLDLKPAQVPSIPVPEPEAMLASAPVVTRAGKGRDIIVVVDAGHGGKDPGALS
QRGDREKDVALIIAQNLARMINQQKGYKAKLVRNDDFFVPLRKRVDVARKYNADMFISVH
ADAAPRRTASGASVYALSEHGATSTTARWLANKENDVDLIGANEILKNKDPVLAGVLLDM
SMNATISSSLDLGDRVLNSLSNVTGLHLKRVEQAGFAVLKSPDIPSILVETGFMSNDRDS
QKLLNPRHQKALAQSIFGGIHHYFSERPPTGTYLSSIKEQATG

Enzyme Prediction     

No EC number prediction in MGYG000001457_01071.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10319	PRK10319	1.39e-66	150	386	46	278	N-acetylmuramoyl-L-alanine amidase AmiA.
COG0860	AmiC	1.49e-64	101	385	2	229	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
PRK10431	PRK10431	2.50e-64	56	388	51	420	N-acetylmuramoyl-l-alanine amidase II; Provisional
cd02696	MurNAc-LAA	1.69e-61	164	380	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.
pfam01520	Amidase_3	3.57e-51	165	380	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
SDU26205.1	2.87e-131	5	399	2	409
QMV64163.1	1.06e-128	33	400	31	411
ANI17771.1	2.75e-128	22	399	25	417
AVO52470.1	3.01e-128	33	400	31	411
AMO79068.1	3.12e-128	22	399	29	421

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BIN_A	4.62e-77	27	386	20	395	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A	4.30e-35	165	387	7	227	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A	7.42e-23	163	383	5	177	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A	1.53e-20	165	387	6	185	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A	1.20e-16	164	383	3	175	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P63883	1.21e-77	2	386	9	409	N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli (strain K12) OX=83333 GN=amiC PE=1 SV=1
P63884	1.21e-77	2	386	9	409	N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=amiC PE=3 SV=1
Q9K0V3	2.32e-62	30	385	37	409	N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1
P26366	1.49e-57	72	388	64	414	N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P26365	1.44e-54	157	388	186	420	N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as TAT

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000258	0.005727	0.000054	0.992239	0.001698	0.000015

TMHMM  Annotations     

start	end
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