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UniProtKB/Swiss-Prot entry A1TKD3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DDL_ACIAC
Primary accession number A1TKD3
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 21)
Name and origin of the protein
Protein name D-alanine--D-alanine ligase
Synonyms EC 6.3.2.4
D-alanylalanine synthetase
D-Ala-D-Ala ligase
Gene name
Name: ddl
OrderedLocusNames: Aave_0823
From
Acidovorax avenae subsp. citrulli (strain AAC00-1) [TaxID: 397945] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Acidovorax.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
Comments
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
CP000512; ABM31421.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_969195.1; -.
3D structure databases
ModBase A1TKD3.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
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).
BLOCKS A1TKD3.
ProtoNet A1TKD3.
Genome annotation databases
GeneID 4668635; -.
GenomeReviews CP000512_GR; Aave_0823.
KEGG aav:Aave_0823; -.
NMPDR fig|397945.5.peg.714; -.
CMR A1TKD3; Aave_0823.
Other
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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   334  334     D-alanine--D-alanine ligase. PRO_0000341044
DOMAIN   114   314  201     ATP-grasp. 
NP_BIND   140   195  56     ATP (By similarity). 
METAL   267   267        Magnesium or manganese 1 (By similarity). 
METAL   281   281        Magnesium or manganese 1 (By similarity). 
METAL   281   281        Magnesium or manganese 2 (By similarity). 
METAL   283   283        Magnesium or manganese 2 (By similarity). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 35911 Da [This is the MW of the unprocessed precursor] CRC64: FD262C90DC540D1A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAGLPETEI DVRALGKVAV LMGGDSAERE VSLMSGGGVL QALRARGVDA HAFDPSQSDL 

        70         80         90        100        110        120 
SELKSHGYAR CFIALHGRHG EDGTVQGALE LLGIPYTGPG VMASAIAMDK IMTKRIWRFE 

       130        140        150        160        170        180 
GLPTPDWRLV SSAAETAQAL EDLGSPMIVK PSREGSTIGL TKVTSPGQCE QAYRLASRYD 

       190        200        210        220        230        240 
PEVLCEQFIE GEETTCPVLG QGAGAHALPV IRIVAPEGNY DYQNKYFTDV TQYHCPCGLP 

       250        260        270        280        290        300 
EQEEREIQRL VVEAFRTLQC RGWARADIMI RASDRKPFLL EINTSPGMTG HSLVPMSARA 

       310        320        330 
MGVSYEELCL RILAGASLDA RQGQVDAAGH PGAA 

A1TKD3 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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