P0A6J8 (DDLA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-alanine--D-alanine ligase A
EC=6.3.2.4

Alternative name(s):
D-Ala-D-Ala ligase A
D-alanylalanine synthetase A

Gene names

Name:	ddlA
Ordered Locus Names:	b0381, JW0372

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation. HAMAP-Rule MF_00047
Catalytic activity	ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP-Rule MF_00047
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047
Subcellular location	Cytoplasm HAMAP-Rule MF_00047.
Sequence similarities	Belongs to the D-alanine--D-alanine ligase family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell wall Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP D-alanine-D-alanine ligase activity Inferred from direct assay PubMed 1554356Ref.1. Source: EcoliWiki magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	D-alanine--D-alanine ligase A HAMAP-Rule MF_00047		PRO_0000177815
Regions
	Domain	145 – 348	204	ATP-grasp
	Nucleotide binding	175 – 230	56	ATP By similarity
Sites
	Metal binding	302	1	Magnesium or manganese 1 By similarity
	Metal binding	315	1	Magnesium or manganese 1 By similarity
	Metal binding	315	1	Magnesium or manganese 2 By similarity
	Metal binding	317	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A6J8 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: C7FDBEC353AC1320	FASTA	364	39,316
	10 20 30 40 50 60 MEKLRVGIVF GGKSAEHEVS LQSAKNIVDA IDKSRFDVVL LGIDKQGQWH VSDASNYLLN 70 80 90 100 110 120 ADDPAHIALR PSATSLAQVP GKHEHQLIDA QNGQPLPTVD VIFPIVHGTL GEDGSLQGML 130 140 150 160 170 180 RVANLPFVGS DVLASAACMD KDVTKRLLRD AGLNIAPFIT LTRANRHNIS FAEVESKLGL 190 200 210 220 230 240 PLFVKPANQG SSVGVSKVTS EEQYAIAVDL AFEFDHKVIV EQGIKGREIE CAVLGNDNPQ 250 260 270 280 290 300 ASTCGEIVLT SDFYAYDTKY IDEDGAKVVV PAAIAPEIND KIRAIAVQAY QTLGCAGMAR 310 320 330 340 350 360 VDVFLTPENE VVINEINTLP GFTNISMYPK LWQASGLGYT DLITRLIELA LERHAADNAL KTTM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Existence of two D-alanine:D-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes." Zawadzke L.E., Bugg T.D., Walsh C.T. Biochemistry 30:1673-1682(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M58467 Genomic DNA. Translation: AAA23671.1. U73857 Genomic DNA. Translation: AAB18104.1. U00096 Genomic DNA. Translation: AAC73484.1. AP009048 Genomic DNA. Translation: BAE76162.1.
PIR	CEECDA. A39182.
RefSeq	NP_414915.1. NC_000913.2. YP_488674.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A6J8.
SMR	P0A6J8. Positions 3-363.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47939N.
IntAct	P0A6J8. 13 interactions.
STRING	511145.b0381.
Proteomic databases
PaxDb	P0A6J8.
PRIDE	P0A6J8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73484; AAC73484; b0381. BAE76162; BAE76162; BAE76162.
GeneID	12932537. 945313.
KEGG	ecj:Y75_p0370. eco:b0381.
PATRIC	32115903. VBIEscCol129921_0393.
Organism-specific databases
EchoBASE	EB0209.
EcoGene	EG10213. ddlA.
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000011593.
KO	K01921.
OMA	LLHGPFG.
ProtClustDB	PRK01966.
Enzyme and pathway databases
BioCyc	EcoCyc:DALADALALIGA-MONOMER. ECOL316407:JW0372-MONOMER. MetaCyc:DALADALALIGA-MONOMER.
UniPathway	UPA00219.
Gene expression databases
Genevestigator	P0A6J8.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 1 hit. 3.40.50.20. 1 hit.
HAMAP	MF_00047. Dala_Dala_lig.
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR000291. D-Ala_lig_Van_CS. IPR005905. D_ala_D_ala. IPR011095. Dala_Dala_lig_C. IPR011127. Dala_Dala_lig_N. IPR016185. PreATP-grasp_dom. [Graphical view]
PANTHER	PTHR23132. PTHR23132. 1 hit.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 1 hit. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit.
TIGRFAMs	TIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00843. DALA_DALA_LIGASE_1. 1 hit. PS00844. DALA_DALA_LIGASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00260. Cycloserine.

Entry information

Entry name

DDLA_ECOLI

Accession

Primary (citable) accession number: P0A6J8
Secondary accession number(s): P23844, Q2MC44

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program