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F4M5H9

- F4M5H9_ECOLX

UniProt

F4M5H9 - F4M5H9_ECOLX

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Protein

D-alanine--D-alanine ligase

Gene
ddl, UMNK88_429
Organism
Escherichia coli UMNK88
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Cell wall formation By similarity.UniRule annotationSAAS annotations

Catalytic activityi

ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.UniRule annotationSAAS annotations

Cofactori

Binds 2 magnesium or manganese ions per subunit By similarity.UniRule annotationSAAS annotations

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi302 – 3021Magnesium or manganese 1 By similarityUniRule annotation
Metal bindingi315 – 3151Magnesium or manganese 1 By similarityUniRule annotation
Metal bindingi315 – 3151Magnesium or manganese 2 By similarityUniRule annotation
Metal bindingi317 – 3171Magnesium or manganese 2 By similarityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 23056ATP By similarityUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. D-alanine-D-alanine ligase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  2. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationSAAS annotationsImported

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradationUniRule annotationSAAS annotations, Peptidoglycan synthesisUniRule annotationSAAS annotations

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotations, MagnesiumUniRule annotationSAAS annotations, ManganeseUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL696406:GJE4-420-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--D-alanine ligaseUniRule annotation (EC:6.3.2.4UniRule annotation)
Alternative name(s):
D-Ala-D-Ala ligase
D-alanylalanine synthetase
Gene namesi
Name:ddlUniRule annotation
ORF Names:UMNK88_429Imported
OrganismiEscherichia coli UMNK88Imported
Taxonomic identifieri696406 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008464: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotationSAAS annotations

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotations

PTM / Processingi

Proteomic databases

PRIDEiF4M5H9.

Structurei

3D structure databases

ProteinModelPortaliF4M5H9.
SMRiF4M5H9. Positions 3-363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 348204ATP-grasp By similarityUniRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.UniRule annotation
Contains ATP-grasp domain.SAAS annotations

Phylogenomic databases

KOiK01921.
OMAiQIDVIFP.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_00047. Dala_Dala_lig.
InterProiIPR011761. 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]
PANTHERiPTHR23132. PTHR23132. 1 hit.
PfamiPF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
PS00844. DALA_DALA_LIGASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F4M5H9-1 [UniParc]FASTAAdd to Basket

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MEKLRVGIVF GGKSAEHEVS LQSAKNIVDA IDKSRFDVVL LGIDKQGQWH    50
VSDASNYLLN ADDPAHIALR PSATSLAQVP GKHEHQLIDA QNGQPLPTVD 100
VIFPIVHGTL GEDGSLQGML RVANLPFVGS DVLASAACMD KDVTKRLLRD 150
AGLNIAPFIT LTRANRHNIS FAEVESKLGL PLFVKPANQG SSVGVSKVTS 200
EEQYAIAVDL AFEFDHKVIV EQGIKGREIE CAVLGNDNPQ ASTCGEIVLT 250
SDFYAYDTKY IDEDGAKVVV PAAIAPEIND KIRAIAVQAY QTLGCAGMAR 300
VDVFLTPENE VVINEINTLP GFTNISMYPK LWQASGLGYT DLITRLIELA 350
LERHAADNAL KTTM 364
Length:364
Mass (Da):39,316
Last modified:June 28, 2011 - v1
Checksum:iC7FDBEC353AC1320
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002729 Genomic DNA. Translation: AEE55076.1.
RefSeqiYP_006132239.1. NC_017641.1.

Genome annotation databases

EnsemblBacteriaiAEE55076; AEE55076; UMNK88_429.
GeneIDi12683723.
KEGGieun:UMNK88_429.
PATRICi48568536. VBIEscCol159162_0417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002729 Genomic DNA. Translation: AEE55076.1 .
RefSeqi YP_006132239.1. NC_017641.1.

3D structure databases

ProteinModelPortali F4M5H9.
SMRi F4M5H9. Positions 3-363.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi F4M5H9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEE55076 ; AEE55076 ; UMNK88_429 .
GeneIDi 12683723.
KEGGi eun:UMNK88_429.
PATRICi 48568536. VBIEscCol159162_0417.

Phylogenomic databases

KOi K01921.
OMAi QIDVIFP.

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci ECOL696406:GJE4-420-MONOMER.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPi MF_00047. Dala_Dala_lig.
InterProi 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 ]
PANTHERi PTHR23132. PTHR23132. 1 hit.
Pfami PF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
PS00844. DALA_DALA_LIGASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome structure of porcine enterotoxigenic Escherichia coli."
    Johnson T.J., Shepard S.M., Isaacson R.E.
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: UMNK88Imported.

Entry informationi

Entry nameiF4M5H9_ECOLX
AccessioniPrimary (citable) accession number: F4M5H9
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 11, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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