[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00220a033; PubMed=1993184 [NCBI, ExPASy, EBI, Israel, Japan] Zawadzke L.E., Bugg T.D., Walsh C.T.; "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."; Biochemistry 30:1673-1682(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; 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.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

FUNCTION: Cell wall formation.
CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.
COFACTOR: Binds 2 magnesium or manganese ions per subunit (By similarity).
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
SIMILARITY: Contains 1 ATP-grasp domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M58467; AAA23671.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18104.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73484.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76162.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39182; CEECDA.

RefSeq

AP_001032.1; -.
NP_414915.1; -.

3D structure databases

HSSP

P25051; 1E4E. [HSSP ENTRY / PDB]

ModBase

P0A6J8.

Enzyme and pathway databases

BioCyc

EcoCyc:DALADALALIGA-MON; -.
MetaCyc:DALADALALIGA-MON; -.

Organism-specific databases

EchoBASE

EB0209; -.

EcoGene

EG10213; ddlA.

Ontologies

GO:0005618;	Cellular component: cell wall (inferred from electronic annotation from InterPro).
GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008716;	Molecular function: D-alanine-D-alanine ligase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00047; -; 1.
PBIL [Tree]

InterPro

IPR011761; ATP-grasp.
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.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.

Pfam

PF07478; Dala_Dala_lig_C; 1.
PF01820; Dala_Dala_lig_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01205; D_ala_D_alaTIGR; 1.

PROSITE

PS50975; ATP_GRASP; 1.
PS00843; DALA_DALA_LIGASE_1; 1.
PS00844; DALA_DALA_LIGASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

945313; -.

GenomeReviews

AP009048_GR; JW0372.
U00096_GR; b0381.

KEGG

ecj:JW0372; -.
eco:b0381; -.

Phylogenomic databases

HOGENOM

P0A6J8; -.

Other

DrugBank

DB00260; Cycloserine.

Genome annotation databases

CMR

P0A6J8; b0381.

Other

ProtoNet

P0A6J8.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 364`	`364`	`D-alanine--D-alanine ligase A.`	`PRO_0000177815`
`DOMAIN`	`145 348`	`204`	`ATP-grasp.`
`NP_BIND`	`175 230`	`56`	`ATP (By similarity).`
`METAL`	`302 302`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`315 315`		`Magnesium or manganese 1 (By similarity).`
`METAL`	`315 315`		`Magnesium or manganese 2 (By similarity).`
`METAL`	`317 317`		`Magnesium or manganese 2 (By similarity).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39316 Da [This is the MW of the unprocessed precursor]

CRC64: C7FDBEC353AC1320 [This is a checksum on the sequence]

        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

P0A6J8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools