Reviewed, UniProtKB/Swiss-Prot P30013 (AMPD_SALTY)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW 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 zinc 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
	Metal binding	34	1	Zinc; catalytic By similarity
	Metal binding	154	1	Zinc; catalytic By similarity
	Metal binding	164	1	Zinc; catalytic By similarity
Experimental info
	Sequence conflict	158	1	T → A in CAB89835. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P30013-1 [UniParc]. Last modified December 19, 2001. Version 3. 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]	"Characterization of a Salmonella-specific region located between ampE and aroP genes." Cano D., Casadesus J., Garcia-del Portillo F. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SL1344.
[2]	"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: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"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: 8419294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95. Strain: LT2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ242516 Genomic DNA. Translation: CAB89835.1. AE006468 Genomic DNA. Translation: AAL19110.1. L07292 Genomic DNA. Translation: AAA03224.1.
RefSeq	NP_459151.1.
3D structure databases
HSSP	HSSP built from PDB template 1J3G based on UniProtKB P82974.
SMR	P30013. Positions 1-187.
ModBase	Search...
Genome annotation databases
GeneID	1251664.
GenomeReviews	Gene locus STM0146 in contig AE006468_GR.
KEGG	stm:STM0146.
NMPDR	fig|99287.1.peg.144.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P30013.
OMA	VQFVSCD.
Enzyme and pathway databases
BioCyc	STYP99287:STM0146-MON.
Family and domain databases
InterPro	IPR002502. Amidase_2. [Graphical view]
Gene3D	G3DSA:3.40.80.10. Amidase_2. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPD_SALTY

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	December 19, 2001
Last modified:	November 3, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)