P0CL03 (AMPD_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
EC=3.5.1.28

Alternative name(s):
N-acetylmuramoyl-L-alanine amidase

Gene names

Name:	ampD
Ordered Locus Names:	STM0146

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety By similarity.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Cofactor	Zinc; required for amidase activity By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 187	187	1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD		PRO_0000164415
Sites
	Active site	116	1	Proton acceptor By similarity
	Metal binding	34	1	Zinc; catalytic By similarity
	Metal binding	154	1	Zinc; catalytic By similarity
	Metal binding	164	1	Zinc; catalytic By similarity
	Site	162	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0CL03 [UniParc]. Last modified March 8, 2011. Version 1. Checksum: 9E7EBAC553BA8EA4	FASTA	187	20,943
	10 20 30 40 50 60 MLPDKGWLVE ARRVPSPHYD CRPDDEKPSL LVVHNISLPP GEFGGPWIDA LFTGTIDPDA 70 80 90 100 110 120 HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS NYQGRERCND FSIGIELEGT 130 140 150 160 170 180 DTLAYTDAQY QQLAAVTRTL IASYPAIADN MTGHCNITPD RKTDPGPAFD WPRFRALVAL SSHKEMT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"The Salmonella typhimurium nadC gene: sequence determination by use of Mud-P22 and purification of quinolinate phosphoribosyltransferase." Hughes K.T., Dessen A., Gray J.P., Grubmeyer C. J. Bacteriol. 175:479-486(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95. Strain: LT2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006468 Genomic DNA. Translation: AAL19110.1. L07292 Genomic DNA. Translation: AAA03224.1.
RefSeq	NP_459151.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P0CL03.
SMR	P0CL03. Positions 1-187.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL19110; AAL19110; STM0146.
GeneID	1251664.
KEGG	stm:STM0146.
PATRIC	32378571. VBISalEnt20916_0155.
Phylogenomic databases
HOGENOM	HOG000255963.
KO	K03806.
OMA	CNDDSIG.
Family and domain databases
Gene3D	3.40.80.10. 1 hit.
InterPro	IPR002502. Amidase_domain. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
SUPFAM	SSF55846. Amidase_2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMPD_SALTY

Accession

Primary (citable) accession number: P0CL03
Secondary accession number(s): P30013, Q9L4I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 8, 2011
Last sequence update:	March 8, 2011
Last modified:	May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program