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Protein

D-alanine--D-alanine ligase

Gene

ddlA

Organism
Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Cell wall formation.UniRule annotationSAAS annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationSAAS annotation, Mn2+UniRule annotationSAAS annotationNote: Binds 2 magnesium or manganese ions per subunit.UniRule annotationSAAS annotation
  • Mg2+, Mn2+Note: Binds 2 magnesium or manganese ions per subunit.

Pathway: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotationSAAS annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Pathway: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi283 – 2831Magnesium or manganese 1UniRule annotation
Metal bindingi296 – 2961Magnesium or manganese 1UniRule annotation
Metal bindingi296 – 2961Magnesium or manganese 2UniRule annotation
Metal bindingi298 – 2981Magnesium or manganese 2UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi154 – 20956ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationSAAS annotation

Keywords - Biological processi

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

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciSVIO637905:GCRO-2518-MONOMER.
UniPathwayiUPA00219.
UPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--D-alanine ligaseUniRule annotationSAAS annotation (EC:6.3.2.4UniRule annotationSAAS annotation)
Alternative name(s):
D-Ala-D-Ala ligaseUniRule annotation
D-alanylalanine synthetaseUniRule annotation
Gene namesi
Name:ddlAImported
Synonyms:ddlUniRule annotationImported
Ordered Locus Names:SVI_2416Imported
OrganismiShewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12)Imported
Taxonomic identifieri637905 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002350 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Protein-protein interaction databases

STRINGi637905.SVI_2416.

Structurei

3D structure databases

ProteinModelPortaliD4ZL38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 329206ATP-graspUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the D-alanine--D-alanine ligase family.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000011592.
KOiK01921.
OMAiWFPILHG.

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]
PIRSFiPIRSF039102. Ddl/VanB. 1 hit.
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.

D4ZL38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTNLLLIC GGGGDEHAIS LMSAKFFETS LAKLAHINLL KIELDAQGHY
60 70 80 90 100
RTQAGELCEL TNRKQIRFDD VNKASWPVDY VIPCIHGYPG ETGDIQSYFE
110 120 130 140 150
LIKLPYFGCD SEASRNCFNK VTAKMWFSAL GIPNTPYIFL NDFNDDAINQ
160 170 180 190 200
AQQALASWGS IFIKAASQGS SVGCYRVDSP EELTESLKQA FTYSPYVIVE
210 220 230 240 250
KTIEARELEV AVYEKDGEII ATQPGEIICG TNTFYTFDEK YAENSQAETK
260 270 280 290 300
VVADISESVS QEIREYAVKV FKGMKLSHLS RIDFFLTADN EILLNEINTF
310 320 330
PGLTPISMFP KMLQNHGDNF SDYLNHNIMQ QLSKKD
Length:336
Mass (Da):37,711
Last modified:June 15, 2010 - v1
Checksum:i3A02D07EBF5F1C27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011177 Genomic DNA. Translation: BAJ02387.1.
RefSeqiWP_013051691.1. NC_014012.1.
YP_003557165.1. NC_014012.1.

Genome annotation databases

EnsemblBacteriaiBAJ02387; BAJ02387; SVI_2416.
KEGGisvo:SVI_2416.
PATRICi35461075. VBISheVio92117_2333.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011177 Genomic DNA. Translation: BAJ02387.1.
RefSeqiWP_013051691.1. NC_014012.1.
YP_003557165.1. NC_014012.1.

3D structure databases

ProteinModelPortaliD4ZL38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi637905.SVI_2416.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAJ02387; BAJ02387; SVI_2416.
KEGGisvo:SVI_2416.
PATRICi35461075. VBISheVio92117_2333.

Phylogenomic databases

HOGENOMiHOG000011592.
KOiK01921.
OMAiWFPILHG.

Enzyme and pathway databases

UniPathwayiUPA00219.
UPA00219.
BioCyciSVIO637905:GCRO-2518-MONOMER.

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]
PIRSFiPIRSF039102. Ddl/VanB. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence and comparative analysis of Shewanella violacea, a psychrophilic and piezophilic bacterium from deep sea floor sediments."
    Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T., Nakasone K., Mori H.
    Mol. Biosyst. 6:1216-1226(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10179 / CIP 106290 / LMG 19151 / DSS12Imported.

Entry informationi

Entry nameiD4ZL38_SHEVD
AccessioniPrimary (citable) accession number: D4ZL38
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 24, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.