CAZyme Information: MGYG000002463_05975

Basic Information

• Species: Pseudomonas aeruginosa
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas; Pseudomonas aeruginosa
• CAZyme ID: MGYG000002463_05975
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase AmiC

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
397	MGYG000002463_79|CGC3	42934.45	10.9623

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002463	6750396	Isolate	Brazil	South America

• Gene Location: Start: 136282; End: 137475 Strand: -

Full Sequence      

MKRRRLLQSLLAGLALQPFLAASANVRIRQARAWNSSESWRLVLELDGPPRYRTFSLQAP
ERLILDLPDAQLLATLSELPLDGPVRAIRSGQLGGGGTRIVLDLRQAVRPRSFALEPQAG
KGHRLVLDLYPQALAAPPEPMLALARPLPSTGRDILVVVDAGHGGKDPGAVGSKGEREKD
VALAIARLLARRIDREKGFKARLVRNGDVFVPLRKRPEVARRYNADMFVSVHADAAPRLT
ASGASVYALSEHGASSTMARWMADRENGADLIGNSGNLPLQGRDKVLAGVILDMALSSTI
ASSLDLGHSVLGQLSDVTALHQKRVEQAGFAVLKSPDIPSILVETGFISNRGDCRRLMDE
RHRQRLAEAIFVGVQGYFRQRPPAGSYLAALSAQPPG

Enzyme Prediction     

No EC number prediction in MGYG000002463_05975.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10431	PRK10431	4.91e-76	35	397	32	440	N-acetylmuramoyl-l-alanine amidase II; Provisional
PRK10319	PRK10319	2.95e-73	125	378	24	276	N-acetylmuramoyl-L-alanine amidase AmiA.
COG0860	AmiC	6.78e-73	99	381	2	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696	MurNAc-LAA	2.02e-61	157	375	2	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.
pfam01520	Amidase_3	3.26e-52	157	374	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
QGW79568.1	5.81e-124	22	391	21	407
AIL63935.1	1.65e-123	22	391	21	407
BBT38187.1	1.93e-123	22	391	21	412
AYN98057.1	1.99e-123	22	391	21	414
AYN18245.1	1.99e-123	22	391	21	414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BIN_A	1.41e-80	25	378	19	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A	2.15e-31	157	381	7	227	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A	2.41e-21	155	380	5	180	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A	2.06e-14	157	377	6	181	ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A	1.11e-13	156	377	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	2.90e-80	3	378	10	407	N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli (strain K12) OX=83333 GN=amiC PE=1 SV=1
P63884	2.90e-80	3	378	10	407	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	8.40e-65	15	377	19	407	N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1
P26366	7.87e-60	42	397	72	433	N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P26365	1.36e-58	35	382	32	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
0.007670	0.025893	0.004589	0.916822	0.044788	0.000220

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002463_05975.