ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8PDW3


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DDLA_XANCP
Primary accession number Q8PDW3
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
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
Synonyms: ddlB
OrderedLocusNames: XCC0222
From
Xanthomonas campestris pv. campestris [TaxID: 340] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
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
AE012118; AAM39541.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_635617.2; -.
3D structure databases
HSSP P25051; 1E4E. [HSSP ENTRY / PDB]
ModBase Q8PDW3.
Enzyme and pathway databases
BioCyc XCAM190485:XCC0222-MON; -.
Ontologies
GO
GO:0005618; Cellular component: cell wall (inferred from electronic annotation from InterPro).
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
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).
Genome annotation databases
GeneID 999929; -.
GenomeReviews AE008922_GR; XCC0222.
KEGG xcc:XCC0222; -.
Phylogenomic databases
HOGENOM Q8PDW3; -.
Genome annotation databases
CMR Q8PDW3; XCC0222.
Other
ProtoNet Q8PDW3.
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   373  373     D-alanine--D-alanine ligase A. PRO_0000177908
DOMAIN   150   353  204     ATP-grasp. 
NP_BIND   180   235  56     ATP (By similarity). 
METAL   307   307        Magnesium or manganese 1 (By similarity). 
METAL   320   320        Magnesium or manganese 1 (By similarity). 
METAL   320   320        Magnesium or manganese 2 (By similarity). 
METAL   322   322        Magnesium or manganese 2 (By similarity). 
Sequence information
Length: 373 AA [This is the length of the unprocessed precursor] Molecular weight: 40110 Da [This is the MW of the unprocessed precursor] CRC64: 01E285702AF9D15F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTGAGMRRIR VGLIFGGKSA EHEVSLQSAR NILQALDPQR FEPVLIGIDK QGQWHLSAQE 

        70         80         90        100        110        120 
SFLLDADDPS RIALRHSGRG LAVLPGAASA QLRAVDAEQA LAQIDVVFPI VHGTLGEDGS 

       130        140        150        160        170        180 
LQGLLRMANL PFVGSGVLGS AVAMDKDMAK RVLRDAGLEV APFACFTRHT AAQADVQTLI 

       190        200        210        220        230        240 
AQFGLPLFVK PANQGSSVGV SQVRSAEEFS AALELALRYD HKVLVEAAIA GREIECAVLG 

       250        260        270        280        290        300 
NATPQASVCG EVVVHDAFYS YQTKYIRDDG AATVIPADID AHTQHRIQQC ALQAYQALDC 

       310        320        330        340        350        360 
AGMARVDVFL CADGRIVINE VNTLPGFTRI SMYPKLWEAS GLDYRSLVTR LIELALERHA 

       370 
DDGRLYSSVV THA 

Q8PDW3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!