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UniProtKB/Swiss-Prot entry Q8PCJ8

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

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Entry information
Entry name DDLB_XANCP
Primary accession number Q8PCJ8
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 44)
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
OrderedLocusNames: XCC0727
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
AE012171; AAM40042.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_636118.1; -.
3D structure databases
HSSP P07862; 1IOW. [HSSP ENTRY / PDB]
ModBase Q8PCJ8.
Enzyme and pathway databases
BioCyc XCAM190485:XCC0727-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 1001363; -.
GenomeReviews AE008922_GR; XCC0727.
KEGG xcc:XCC0727; -.
Phylogenomic databases
HOGENOM Q8PCJ8; -.
Genome annotation databases
CMR Q8PCJ8; XCC0727.
Other
ProtoNet Q8PCJ8.
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   318  318     D-alanine--D-alanine ligase B. PRO_0000177909
DOMAIN   117   315  199     ATP-grasp. 
NP_BIND   146   201  56     ATP (By similarity). 
METAL   268   268        Magnesium or manganese 1 (By similarity). 
METAL   282   282        Magnesium or manganese 1 (By similarity). 
METAL   282   282        Magnesium or manganese 2 (By similarity). 
METAL   284   284        Magnesium or manganese 2 (By similarity). 
Sequence information
Length: 318 AA [This is the length of the unprocessed precursor] Molecular weight: 33569 Da [This is the MW of the unprocessed precursor] CRC64: 82B6E6AEEB93E1A0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTQIAPARI SDPAAFGRVA VLLGGTSSER EVSLNSGSNV LDALRARGVD AQPVDGIPAL 

        70         80         90        100        110        120 
AQALVAQRFD RVFNVLHGHN GGGEDGIVQG LMEAFGVPYT GSNVLGSALS MDKIRTKQVW 

       130        140        150        160        170        180 
LSLGLSTPRY ARLAAGASAQ QIHAAAEQIG LPVIVKPANE GSSVGVSRVF DQAQLDEAVT 

       190        200        210        220        230        240 
LAARYDGALL MEQLIEGDEL TVAVLGDVAL PSIRIVPKGQ WYDYNAKYIA EDTQYLCPGL 

       250        260        270        280        290        300 
DGDAEAQIGQ LALDAFRAAG CSGWGRVDVM RDGSTGQLYL LEVNTAPGMT SHSLVPKAAR 

       310 
QLGIDFEALV WRVLEQTL
Q8PCJ8 in FASTA format

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