D-alanine--D-alanine ligase - Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1)

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C9QS62 (C9QS62_ECOD1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 31. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
D-alanine--D-alanine ligase HAMAP-Rule MF_00047
EC=6.3.2.4 HAMAP-Rule MF_00047

Alternative name(s):
D-Ala-D-Ala ligase HAMAP-Rule MF_00047
D-alanylalanine synthetase HAMAP-Rule MF_00047

Gene names

Name:	ddlB EMBL BAJ41945.1
Synonyms:	ddl HAMAP-Rule MF_00047
Ordered Locus Names:	EcDH1_3508, ECDH1ME8569_0089 EMBL BAJ41945.1

Organism

Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1) [Complete proteome] [HAMAP] EMBL ACX41123.1

Taxonomic identifier

536056 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation By similarity. HAMAP-Rule MF_00047 SAAS SAAS005905
Catalytic activity	ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP-Rule MF_00047 SAAS SAAS005905
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity. SAAS SAAS005905
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047 SAAS SAAS005905
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00047 SAAS SAAS005905.
Sequence similarities	Belongs to the D-alanine--D-alanine ligase family. HAMAP-Rule MF_00047 Contains 1 ATP-grasp domain. HAMAP-Rule MF_00047 SAAS SAAS005905

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation HAMAP-Rule MF_00047 SAAS SAAS005905 Peptidoglycan synthesis HAMAP-Rule MF_00047 SAAS SAAS005905
Cellular component	Cytoplasm HAMAP-Rule MF_00047 SAAS SAAS005905
Ligand	ATP-binding HAMAP-Rule MF_00047 SAAS SAAS005905 Magnesium HAMAP-Rule MF_00047 SAAS SAAS005905 Manganese HAMAP-Rule MF_00047 SAAS SAAS005905 Metal-binding HAMAP-Rule MF_00047 SAAS SAAS005905 Nucleotide-binding
Molecular function	Ligase HAMAP-Rule MF_00047 SAAS SAAS005905 EMBL ACX41123.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell wall Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Domain

101 – 303

203

ATP-grasp By similarity HAMAP-Rule MF_00047

Nucleotide binding

134 – 189

ATP By similarity HAMAP-Rule MF_00047

Sites

Metal binding

257

Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047

Metal binding

270

Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047

Metal binding

270

Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047

Metal binding

272

Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047

Sequences

Sequence

Length

Mass (Da)

Tools

C9QS62 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: F2D401C323A04471
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FASTA

306

32,840

        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

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References

[1]

"Complete sequence of Escherichia coli DH1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Keasling J.D.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1.

[2]

"Comparison of sequence reads obtained from three next-generation sequencing platforms."
Suzuki S., Ono N., Furusawa C., Ying B.W., Yomo T.
PLoS ONE 6:E19534-E19534(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1 and DH1 EMBL BAJ41945.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001637 Genomic DNA. Translation: ACX41123.1. AP012030 Genomic DNA. Translation: BAJ41945.1.
RefSeq	YP_006093412.1. NC_017625.1. YP_006127490.1. NC_017638.1.
3D structure databases
SMR	C9QS62. Positions 1-306.
ModBase	Search...
Proteomic databases
PRIDE	C9QS62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACX41123; ACX41123; EcDH1_3508. BAJ41945; BAJ41945; ECDH1ME8569_0089.
GeneID	12707142. 12873154.
KEGG	edh:EcDH1_3508. edj:ECDH1ME8569_0089.
PATRIC	36699541. VBIEscCol36761_3707.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000011592.
KO	K01921.
OMA	WREAARY.
Enzyme and pathway databases
UniPathway	UPA00219.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 2 hits. 3.40.50.20. 1 hit.
HAMAP	MF_00047. Dala_Dala_lig.
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. 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. IPR016185. PreATP-grasp_dom. [Graphical view]
PANTHER	PTHR23132. PTHR23132. 1 hit.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 2 hits. [Graphical view]
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit.
TIGRFAMs	TIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00843. DALA_DALA_LIGASE_1. 1 hit. PS00844. DALA_DALA_LIGASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C9QS62_ECOD1

Accession

Primary (citable) accession number: C9QS62

Entry history

Integrated into UniProtKB/TrEMBL:	November 24, 2009
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information