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UniProtKB/Swiss-Prot entry P0A6J9

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

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Entry information
Entry name DDLA_ECO57
Primary accession number P0A6J9
Secondary accession number P23844
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on March 29, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 29)
Name and origin of the protein
Protein name D-alanine--D-alanine ligase A
Synonyms EC 6.3.2.4
D-alanylalanine synthetase A
D-Ala-D-Ala ligase A
Gene name
Name: ddlA
OrderedLocusNames: Z0477, ECs0431
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
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., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
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., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
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
AE005174; AAG54727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB33854.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C85533; C85533.
G90682; G90682.
RefSeq NP_286119.1; -.
NP_308458.1; -.
3D structure databases
HSSP P25051; 1E4E. [HSSP ENTRY / PDB]
ModBase P0A6J9.
Enzyme and pathway databases
BioCyc ECOL83334:ECS0431-MON; -.
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:0009252; Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
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 P0A6J9.
Genome annotation databases
GeneID 914533; -.
957325; -.
GenomeReviews BA000007_GR; ECs0431.
AE005174_GR; Z0477.
KEGG ece:Z0477; -.
ecs:ECs0431; -.
Phylogenomic databases
HOGENOM P0A6J9; -.
Genome annotation databases
CMR P0A6J9; Z0477.
Other
ProtoNet P0A6J9.
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   364  364     D-alanine--D-alanine ligase A. PRO_0000177816
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
P0A6J9 in FASTA format

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