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UniProtKB/Swiss-Prot entry P07862


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

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Entry information
Entry name DDLB_ECOLI
Primary accession number P07862
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 96)
Name and origin of the protein
Protein name D-alanine--D-alanine ligase B
Synonyms EC 6.3.2.4
D-alanylalanine synthetase B
D-Ala-D-Ala ligase B
Gene name
Name: ddlB
Synonyms: ddl
OrderedLocusNames: b0092, JW0090
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3528126 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson A.C., Kenan D.J., Sweeney J., Donachie W.D.;
"Further evidence for overlapping transcriptional units in an Escherichia coli cell envelope-cell division gene cluster: DNA sequence and transcriptional organization of the ddl ftsQ region.";
J. Bacteriol. 167:809-817(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/20.13.3305; PubMed=1630901 [NCBI, ExPASy, EBI, Israel, Japan]
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
STRAIN=K12;
DOI=10.1093/nar/18.13.4014; PubMed=2197603 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
"Nucleotide sequence involving murG and murC in the mra gene cluster region of Escherichia coli.";
Nucleic Acids Res. 18:4014-4014(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-306.
PubMed=2228979 [NCBI, ExPASy, EBI, Israel, Japan]
Dewar S.J., Donachie W.D.;
"Regulation of expression of the ftsA cell division gene by sequences in upstream genes.";
J. Bacteriol. 172:6611-6614(1990).
[7]
CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1554356 [NCBI, ExPASy, EBI, Israel, Japan]
Al-Bar O.A., O'Connor C.D., Giles I.G., Akhtar M.;
"D-alanine:D-alanine ligase of Escherichia coli. Expression, purification and inhibitory studies on the cloned enzyme.";
Biochem. J. 282:747-752(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=7939684 [NCBI, ExPASy, EBI, Israel, Japan]
Fan C., Moews P.C., Walsh C.T., Knox J.R.;
"Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3-A resolution.";
Science 266:439-443(1994).
[9]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1021/bi962431t; PubMed=9054558 [NCBI, ExPASy, EBI, Israel, Japan]
Fan C., Park I.-S., Walsh C.T., Knox J.R.;
"D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant.";
Biochemistry 36:2531-2538(1997).
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
M14029; AAA23672.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02668; AAA23815.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52644; CAA36869.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55034; CAA38869.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73203.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96660.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A30289; CEECDL.
RefSeq AP_000755.1; -.
NP_414634.1; -.
3D structure databases
PDB
1IOV; X-ray; 2.20 A; A=1-306.[ExPASy / RCSB / EBI]
1IOW; X-ray; 1.90 A; A=1-306.[ExPASy / RCSB / EBI]
2DLN; X-ray; 2.30 A; A=1-306.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1IOV; -.
1IOW; -.
2DLN; -.
ModBase P07862.
Protein-protein interaction databases
IntAct P07862; -.
Enzyme and pathway databases
BioCyc EcoCyc:DALADALALIGB-MON; -.
MetaCyc:DALADALALIGB-MON; -.
Organism-specific databases
EchoBASE EB0210; -.
EcoGene EG10214; ddlB.
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 P07862.
Genome annotation databases
GeneID 946324; -.
GenomeReviews U00096_GR; b0092.
AP009048_GR; JW0090.
KEGG ecj:JW0090; -.
eco:b0092; -.
Phylogenomic databases
HOGENOM P07862; -.
Other
LinkHub P07862; -.
Genome annotation databases
CMR P07862; b0092.
Other
ProtoNet P07862.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Direct protein sequencing; 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
INIT_MET   1     1        Removed. 
CHAIN   2   306  305     D-alanine--D-alanine ligase B. PRO_0000177818
DOMAIN   101   303  203     ATP-grasp. 
NP_BIND   134   189  56     ATP (By similarity). 
ACT_SITE   15    15         
ACT_SITE   150   150         
ACT_SITE   281   281         
METAL   257   257        Magnesium or manganese 1 (By similarity). 
METAL   270   270        Magnesium or manganese 1 (By similarity). 
METAL   270   270        Magnesium or manganese 2 (By similarity). 
METAL   272   272        Magnesium or manganese 2 (By similarity). 
STRAND   2     7  6      
HELIX   15    31  17      
STRAND   35    39  5      
TURN   41    43  3      
HELIX   46    49  4      
TURN   50    53  4      
STRAND   54    59  6      
TURN   64    66  3      
STRAND   67    69  3      
HELIX   70    78  9      
STRAND   82    84  3      
HELIX   87    93  7      
HELIX   96   105  10      
STRAND   113   117  5      
HELIX   118   121  4      
HELIX   130   133  4      
STRAND   140   144  5      
STRAND   154   156  3      
HELIX   159   161  3      
HELIX   162   169  8      
STRAND   174   180  7      
STRAND   186   192  7      
STRAND   200   203  4      
STRAND   205   209  5      
HELIX   211   215  5      
STRAND   221   225  5      
HELIX   232   245  14      
TURN   246   248  3      
STRAND   251   259  9      
STRAND   265   273  9      
HELIX   281   288  8      
HELIX   293   301  9      
Sequence information
Length: 306 AA [This is the length of the unprocessed precursor] Molecular weight: 32840 Da [This is the MW of the unprocessed precursor] CRC64: F2D401C323A04471 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTDKIAVLLG GTSAEREVSL NSGAAVLAGL REGGIDAYPV DPKEVDVTQL KSMGFQKVFI 

        70         80         90        100        110        120 
ALHGRGGEDG TLQGMLELMG LPYTGSGVMA SALSMDKLRS KLLWQGAGLP VAPWVALTRA 

       130        140        150        160        170        180 
EFEKGLSDKQ LAEISALGLP VIVKPSREGS SVGMSKVVAE NALQDALRLA FQHDEEVLIE 

       190        200        210        220        230        240 
KWLSGPEFTV AILGEEILPS IRIQPSGTFY DYEAKYLSDE TQYFCPAGLE ASQEANLQAL 

       250        260        270        280        290        300 
VLKAWTTLGC KGWGRIDVML DSDGQFYLLE ANTSPGMTSH SLVPMAARQA GMSFSQLVVR 


ILELAD 

P07862 in FASTA format

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