D-alanine--D-alanine ligase - Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W)

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E0IYT7 (E0IYT7_ECOLW) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 25. 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 ADT73642.1
Synonyms:	ddl HAMAP-Rule MF_00047
Ordered Locus Names:	ECW_m0091 EMBL ADT73642.1, WFL_00445 EMBL AFH09758.1
ORF Names:	EschWDRAFT_1494 EMBL EFN38934.1

Organism

Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W) [Complete proteome] [HAMAP] EMBL EFN38934.1

Taxonomic identifier

566546 [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 EFN38934.1
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

E0IYT7 [UniParc].

Last modified November 2, 2010. 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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The draft genome of Escherichia coli W." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Tremaine M., Landick R., Keating D., Woyke T.J. Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: W EMBL EFN38934.1.
[2]	"The genome sequence of E. coli W (ATCC 9637): comparative genome analysis and an improved genome-scale reconstruction of E. coli." Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y., Nielsen L.K. BMC Genomics 12:9-9(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W and W EMBL ADT73642.1.
[3]	"Optical mapping and sequencing of the Escherichia coli KO11 genome reveal extensive chromosomal rearrangements, and multiple tandem copies of the Zymomonas mobilis pdc and adhB genes." Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L., Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O. J. Ind. Microbiol. Biotechnol. 39:629-639(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9637 / CCM 2024 / DSM 1116 / NCIMB 8666 / NRRL B-766 / W and W EMBL AFH09758.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002185 Genomic DNA. Translation: ADT73642.1. CP002967 Genomic DNA. Translation: AFH09758.1. AEDF01000005 Genomic DNA. Translation: EFN38934.1.
RefSeq	YP_006122884.1. NC_017635.1. YP_006171544.1. NC_017664.1.
3D structure databases
SMR	E0IYT7. Positions 1-306.
ModBase	Search...
Proteomic databases
PRIDE	E0IYT7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADT73642; ADT73642; ECW_m0091. AFH09758; AFH09758; WFL_00445. EFN38934; EFN38934; EschWDRAFT_1494.
GeneID	12693853. 12752232.
KEGG	ell:WFL_00445. elw:ECW_m0091.
PATRIC	41591832. VBIEscCol201000_1635.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K01921.
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

E0IYT7_ECOLW

Accession

Primary (citable) accession number: E0IYT7

Entry history

Integrated into UniProtKB/TrEMBL:	November 2, 2010
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 25 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