D-alanine--D-alanine ligase A - Escherichia coli O157:H7

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Reviewed, UniProtKB/Swiss-Prot P0A6J9 (DDLA_ECO57)

Last modified June 16, 2009. Version 35. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    D-alanine--D-alanine ligase A
    EC=6.3.2.4
Alternative name(s):
    D-alanylalanine synthetase A
    D-Ala-D-Ala ligase A

Gene names

Name:	ddlA
Ordered Locus Names:	Z0477, ECs0431

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

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

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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
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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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 MF_00047

PRO_0000177816

Regions

Domain

145 – 348

204

ATP-grasp

Nucleotide binding

175 – 230

ATP By similarity

Sites

Metal binding

302

Magnesium or manganese 1 By similarity

Metal binding

315

Magnesium or manganese 1 By similarity

Metal binding

315

Magnesium or manganese 2 By similarity

Metal binding

317

Magnesium or manganese 2 By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A6J9-1 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: C7FDBEC353AC1320
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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

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References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W.

Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.

Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

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Cross-references

Sequence databases
	AE005174 Genomic DNA. Translation: AAG54727.1. BA000007 Genomic DNA. Translation: BAB33854.1.
PIR	C85533. G90682.
RefSeq	NP_286119.1. NP_308458.1.
3D structure databases
HSSP	HSSP built from PDB template 1E4E based on UniProtKB P25051.
ModBase	Search...
Genome annotation databases
GeneID	914533. 957325.
GenomeReviews	Gene locus Z0477 in contig AE005174_GR. Gene locus ECs0431 in contig BA000007_GR.
KEGG	ece:Z0477. ecs:ECs0431.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A6J9.
OMA	P0A6J9. GREIECG.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0431-MON.
Family and domain databases
HAMAP	MF_00047. [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]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 1 hit. [Graphical view]
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...

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Entry information

Entry name

DDLA_ECO57

Accession

Primary (citable) accession number: P0A6J9
Secondary accession number(s): P23844

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents