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F7XUC3 (F7XUC3_MIDMI) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended 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:ddlA EMBL AEI89482.1
Synonyms:ddl HAMAP-Rule MF_00047
Ordered Locus Names:midi_01206 EMBL AEI89482.1
OrganismMidichloria mitochondrii (strain IricVA) [Complete proteome] [HAMAP] EMBL AEI89482.1
Taxonomic identifier696127 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesCandidatus MidichloriaceaeCandidatus Midichloria

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00047 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

Contains ATP-grasp domain. SAAS SAAS005905

Ontologies

Keywords
   Biological processCell cycle
Cell division SAAS SAAS005548
Cell shape
Cell wall biogenesis/degradation HAMAP-Rule MF_00047 SAAS SAAS005905
Peptidoglycan synthesis HAMAP-Rule MF_00047 SAAS SAAS005905
   Cellular componentCell membrane SAAS SAAS005548
Cytoplasm SAAS SAAS005905 HAMAP-Rule MF_00047
Membrane
   DomainTransmembrane
Transmembrane helix SAAS SAAS005548
   LigandATP-binding HAMAP-Rule MF_00047 SAAS SAAS005905
Magnesium SAAS SAAS005905 HAMAP-Rule MF_00047
Manganese SAAS SAAS005905 HAMAP-Rule MF_00047
Metal-binding HAMAP-Rule MF_00047 SAAS SAAS005905
Nucleotide-binding
   Molecular functionLigase SAAS SAAS005905 HAMAP-Rule MF_00047 EMBL AEI89482.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

D-alanine-D-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain101 – 301201ATP-grasp By similarity HAMAP-Rule MF_00047
Nucleotide binding130 – 18455ATP By similarity HAMAP-Rule MF_00047

Sites

Metal binding2521Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047
Metal binding2681Magnesium or manganese 1 By similarity HAMAP-Rule MF_00047
Metal binding2681Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047
Metal binding2701Magnesium or manganese 2 By similarity HAMAP-Rule MF_00047

Sequences

Sequence LengthMass (Da)Tools
F7XUC3 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 8635E4385156424D

FASTA57564,744
        10         20         30         40         50         60 
MNKHIVLLVG GVSREREVSQ ISGESVRNAL LSLGYRVTVV DPSENLASEL IKLRPDIVFN 

        70         80         90        100        110        120 
CLHGTFGEGG SIPGLLELLR IPYTHSGVTA SAIAMDKILT KKMAQTCDIN TPKYVKIEKS 

       130        140        150        160        170        180 
ALFTMLEKGE DPMPKPYVIK AVQQGSSIGI YLVIDENSDK PKKAEWTFGE QILVEEYIPG 

       190        200        210        220        230        240 
QELSVAVLND KALGVLELRP KTNFYDYTAK YSDGVTEHVH PAEIPQEVYL EAMKRAEEMH 

       250        260        270        280        290        300 
KALGCRTVSR SDFRYNNIGS ADGLFFLEIN THPGFTNLSI VPDIASRRGI SFEQIIEQLL 

       310        320        330        340        350        360 
KDAKMRNNAV KIAKYTYLDT DVHYGKQISS LLQPAREKPF KKIIRVYILF LLGVAAIFYI 

       370        380        390        400        410        420 
LTKLCTNEVD QFVDKLINKT VISELNICGN IQVSKEEIIN TLDLSLPLEV SYINASHIKE 

       430        440        450        460        470        480 
ELLKNPLIKD VEVKINLPNI LSLLVTERQP FALWFDQKQF HLIDEEGFIV KACVEFQEKE 

       490        500        510        520        530        540 
NKYIIAAGTD SNNQLQNLLD ELKGYSISKK LFAVQLISNR RWNILLKNGL IVKLPENNVK 

       550        560        570 
EALVALDLVL ENYSPSKPFN IIDLRLAPGK VYAVF 

« Hide

References

[1]"Phylogenomic evidence for the presence of a flagellum and cbb(3) oxidase in the free-living mitochondrial ancestor."
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F., Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E., Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.
Mol. Biol. Evol. 28:3285-3296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IricVA EMBL AEI89482.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002130 Genomic DNA. Translation: AEI89482.1.
RefSeqYP_004680168.1. NC_015722.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI89482; AEI89482; midi_01206.
GeneID10914928.
KEGGmmn:midi_01206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01921.

Enzyme and pathway databases

BioCycMMIT696127:GI3H-1205-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPMF_00047. Dala_Dala_lig.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005548. Cell_div_FtsQ/DivIB.
IPR005905. D_ala_D_ala.
IPR011095. Dala_Dala_lig_C.
IPR011127. Dala_Dala_lig_N.
IPR013685. POTRA_FtsQ_type.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERPTHR23132. PTHR23132. 1 hit.
PfamPF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 2 hits.
PF03799. FtsQ. 1 hit.
PF08478. POTRA_1. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF7XUC3_MIDMI
AccessionPrimary (citable) accession number: F7XUC3
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)