CAZyme Information: MGYG000001091_02447

Basic Information

• Species: Citrobacter_A sp009363175
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A sp009363175
• CAZyme ID: MGYG000001091_02447
• CAZy Family: CBM50
• CAZyme Description: N-acetylmuramoyl-L-alanine amidase AmiB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
253		27142.36	6.7017

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001091	4193018	MAG	Sweden	Europe

• Gene Location: Start: 126; End: 887 Strand: +

Full Sequence      

MVIAIDAGHGGQDPGAIGPGGTREKNVTIAVARKLRTLLNADPMFKGVLTRDGDYFISVM
GRSDVARKQNANFLVSIHADAAPNRSATGASVWVLSNRRANSEMANWLEEHEKQSELLGG
AGDVLANSQSDPYLSQAVLDLQFGHSQRVGYDVATNMLGQLERIGSLHKRRPEHASLGVL
RSPDIPSVLVETGFISNHSEERLLASDAYQQQLADAIYKGLRNYFQAHPMQSAPQGSAAQ
TASAATPGESLIN

Enzyme Prediction     

No EC number prediction in MGYG000001091_02447.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10431	PRK10431	0.0	1	253	192	445	N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860	AmiC	3.65e-81	1	228	43	231	N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696	MurNAc-LAA	6.13e-64	2	221	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	3.83e-60	2	235	58	286	N-acetylmuramoyl-L-alanine amidase AmiA.
pfam01520	Amidase_3	1.69e-57	3	221	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
CAX57980.1	2.17e-141	1	246	182	427
QEW33843.1	2.17e-141	1	246	182	427
QBR50196.1	2.17e-141	1	246	182	427
QGU89140.1	4.37e-140	1	249	187	437
BCQ47117.1	4.37e-140	1	235	186	420

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BIN_A	1.15e-48	1	225	174	393	Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A	1.44e-30	3	224	7	223	Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A	1.50e-25	1	226	5	179	ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A	1.97e-19	2	224	3	175	Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
7RAG_B	6.05e-17	3	233	19	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
P26365	3.23e-159	1	253	192	445	N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P26366	4.32e-158	1	248	186	433	N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P44493	1.81e-84	1	221	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	3.06e-59	1	225	5	228	Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
Q8K908	5.08e-54	5	226	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001091_02447.