D-alanine--D-alanine ligase A

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P0A1F1 (DDLA_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	STY0412, t2484

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation By similarity.
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 By similarity.
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
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 electronic annotation. Source: HAMAP 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

Initiator methionine

Removed By similarity

Chain

2 – 364

363

D-alanine--D-alanine ligase A HAMAP-Rule MF_00047

PRO_0000177867

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

Sequences

Sequence

Length

Mass (Da)

Tools

P0A1F1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 00AB43A06746E276
Show »

FASTA

364

39,357

        10         20         30         40         50         60 
MAKLRVGIVF GGKSAEHEVS LQSAKNIVDA IDKTRFDVVL LGIDKAGQWH VNDAENYLQN 

        70         80         90        100        110        120 
ADDPAHIALR PSAISLAQVP GKHQHQLINA QNGQPLPTVD VIFPIVHGTL GEDGSLQGML 

       130        140        150        160        170        180 
RVANLPFVGS DVLSSAACMD KDVAKRLLRD AGLNIAPFIT LTRTNRHAFS FAEVESRLGL 

       190        200        210        220        230        240 
PLFVKPANQG SSVGVSKVAN EAQYQQAVAL AFEFDHKVVV EQGIKGREIE CAVLGNDNPQ 

       250        260        270        280        290        300 
ASTCGEIVLN SEFYAYDTKY IDDNGAQVVV PAQIPSEVND KIRAIAIQAY QTLGCAGMAR 

       310        320        330        340        350        360 
VDVFLTADNE VVINEINTLP GFTNISMYPK LWQASGLGYT DLISRLIELA LERHTANNAL 


KTTM

« Hide

References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P.

Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627266 Genomic DNA. Translation: CAD08835.1. AE014613 Genomic DNA. Translation: AAO70072.1.
RefSeq	NP_806212.1. NC_004631.1.
3D structure databases
ProteinModelPortal	P0A1F1.
ModBase	Search...
Protein-protein interaction databases
STRING	220341.STY0412.
Proteomic databases
PRIDE	P0A1F1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO70072; AAO70072; t2484. CAD08835; CAD08835; CAD08835.
GeneID	1070527.
KEGG	stt:t2484.
PATRIC	18538650. VBISalEnt120419_0409.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000011593.
KO	K01921.
OMA	LLHGPFG.
ProtClustDB	PRK01966.
Enzyme and pathway databases
UniPathway	UPA00219.
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...

Entry information

Entry name

DDLA_SALTI

Accession

Primary (citable) accession number: P0A1F1
Secondary accession number(s): P15051

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents