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UniProtKB/Swiss-Prot entry Q5PBK2

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

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Entry information
Entry name DDL_ANAMM
Primary accession number Q5PBK2
Secondary accession numbers None
Integrated into Swiss-Prot on June 10, 2008
Sequence was last modified on January 4, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 42)
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: AM205
From
Anaplasma marginale (strain St. Maries) [TaxID: 234826] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Anaplasmataceae; Anaplasma.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0406656102; PubMed=15618402 [NCBI, ExPASy, EBI, Israel, Japan]
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins.";
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
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
CP000030; AAV86327.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_153582.1; -.
3D structure databases
ModBase Q5PBK2.
Enzyme and pathway databases
BioCyc AMAR234826:AM205-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; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q5PBK2.
Genome annotation databases
GeneID 3171882; -.
GenomeReviews CP000030_GR; AM205.
KEGG ama:AM205; -.
Phylogenomic databases
HOGENOM Q5PBK2; -.
Genome annotation databases
CMR Q5PBK2; AM205.
Other
ProtoNet Q5PBK2.
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_0000341052
DOMAIN   110   306  197     ATP-grasp. 
NP_BIND   138   190  53     ATP (By similarity). 
METAL   258   258        Magnesium or manganese 1 (By similarity). 
METAL   272   272        Magnesium or manganese 1 (By similarity). 
METAL   272   272        Magnesium or manganese 2 (By similarity). 
METAL   274   274        Magnesium or manganese 2 (By similarity). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 36433 Da [This is the MW of the unprocessed precursor] CRC64: 223FB0FC1F3F40AF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPVSLARNAG MLSVAVLCGG SSPEREVSLA GGKRVADALG RLGYNATVLD LNRESVGQLL 

        70         80         90        100        110        120 
AMAPDLVYNA LHGVQGEDGC VSGLLDILGL ACTHSHVAAS SVGMDKVLTK HVLKSLGIDF 

       130        140        150        160        170        180 
PKFDVLTKEE LLSAKEVLPY PFVIKPVRGG STIGVHAIFS KSEYLDLSAH ADTLEDRMIV 

       190        200        210        220        230        240 
EEYVSGQEVQ TAVFLGRAIG TMELLFEGRI YSYDAKYVEG LCEHIFPANL PYDIYNLTLE 

       250        260        270        280        290        300 
WALKLHQCLG CKTLSRVDFR YDVANKALKL LEINTHPGMT VSSTLPEVLW LRCGLNFDHV 

       310        320        330 
VDLIVQDALG IDDSRRAYID ELMGKTVSRE PSHV
Q5PBK2 in FASTA format

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