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 Q898Z5


[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 DDLB_CLOTE
Primary accession number Q898Z5
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 41)
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: CTC_00291
From
Clostridium tetani [TaxID: 1513] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Massachusetts / E88;
DOI=10.1073/pnas.0335853100; PubMed=12552129 [NCBI, ExPASy, EBI, Israel, Japan]
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
"The genome sequence of Clostridium tetani, the causative agent of tetanus disease.";
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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
AE015927; AAO34934.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_780997.1; -.
3D structure databases
HSSP P71454; 1EHI. [HSSP ENTRY / PDB]
ModBase Q898Z5.
Enzyme and pathway databases
BioCyc CTET212717:CTC_00291-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 Q898Z5.
Genome annotation databases
GeneID 1059868; -.
GenomeReviews AE015927_GR; CTC_00291.
KEGG ctc:CTC00291; -.
NMPDR fig|212717.1.peg.219; -.
Phylogenomic databases
HOGENOM Q898Z5; -.
Genome annotation databases
CMR Q898Z5; CTC_00291.
Other
ProtoNet Q898Z5.
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   358  358     D-alanine--D-alanine ligase B. PRO_0000177810
DOMAIN   147   352  206     ATP-grasp. 
NP_BIND   179   234  56     ATP (By similarity). 
METAL   305   305        Magnesium or manganese 1 (By similarity). 
METAL   319   319        Magnesium or manganese 1 (By similarity). 
METAL   319   319        Magnesium or manganese 2 (By similarity). 
METAL   321   321        Magnesium or manganese 2 (By similarity). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 40536 Da [This is the MW of the unprocessed precursor] CRC64: 36E6E9FA2AF9B8F9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLAQQLNLY ILKGEIIMKK IKIAIVFGGQ STEHEVSRNS VTSILKNINR DKYEICPIGI 

        70         80         90        100        110        120 
TKEGKWFQYT GDINNIKNGQ WEKDNKNKLE NGYNVLFNKE VELVFPVLHG LYGEDGTIQG 

       130        140        150        160        170        180 
LCKLVGLPCV GPGVLSSALC MDKIYTKYVL ENFKFKQANY VVVNKFEYEK NKEEIIKEVE 

       190        200        210        220        230        240 
KLQYDVFIKP ANSGSSVGIT KAHNKEELLK GLEEAFIHDK NVLVEEAINA REIEVAVLGN 

       250        260        270        280        290        300 
DDPKAAVPGE IIPAKEFYDY EAKYQNENSE LLIPANIDNI KQEEIKELAI KIYKLLGCSG 

       310        320        330        340        350 
LARVDFLMDK ESNEVYFNEV NTLPGFTKIS MYPKLWEASG KSYSALIDEL IELAINNK 

Q898Z5 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!