Skip Header

Contribute Send feedback
Read comments (?) or add your own

P39581 (DLTA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-alanine--poly(phosphoribitol) ligase subunit 1
EC=6.1.1.13
Alternative name(s):
D-alanine-D-alanyl carrier protein ligase
Short name=DCL
D-alanine-activating enzyme
Short name=DAE
Gene names
Name:dltA
Synonyms:dae
Ordered Locus Names:BSU38500
ORF Names:ipa-5r
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Catalyzes an ATP-dependent two-step reaction where it forms a high energy D-alanyl AMP intermediate and transfers the alanyl residues from AMP to Dcp. HAMAP-Rule MF_00593

Catalytic activity

ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate). HAMAP-Rule MF_00593

Pathway

Cell wall biogenesis; lipoteichoic acid biosynthesis. HAMAP-Rule MF_00593

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00593.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipoteichoic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionAMP binding

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

D-alanine-poly(phosphoribitol) ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503D-alanine--poly(phosphoribitol) ligase subunit 1 HAMAP-Rule MF_00593
PRO_0000213142

Secondary structure

1 .......................................................................................... 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39581 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 76604AA90C812644

FASTA50355,809
        10         20         30         40         50         60 
MKLLHAIQTH AETYPQTDAF RSQGQSLTYQ ELWEQSDRAA AAIQKRISGE KKSPILVYGH 

        70         80         90        100        110        120 
MEPHMIVSFL GSVKAGHPYI PVDLSIPSER IAKIIESSGA ELLIHAAGLS IDAVGQQIQT 

       130        140        150        160        170        180 
VSAEELLENE GGSVSQDQWV KEHETFYIIY TSGSTGNPKG VQISAANLQS FTDWICADFP 

       190        200        210        220        230        240 
VSGGKIFLNQ APFSFDLSVM DLYPCLQSGG TLHCVTKDAV NKPKVLFEEL KKSGLNVWTS 

       250        260        270        280        290        300 
TPSFVQMCLM DPGFSQDLLP HADTFMFCGE VLPVSVAKAL LERFPKAKIF NTYGPTEATV 

       310        320        330        340        350        360 
AVTSVEITND VISRSESLPV GFAKPDMNIF IMDEEGQPLP EGEKGEIVIA GPSVSRGYLG 

       370        380        390        400        410        420 
EPELTEKAFF SHEGQWAYRT GDAGFIQDGQ IFCQGRLDFQ IKLHGYRMEL EEIEFHVRQS 

       430        440        450        460        470        480 
QYVRSAVVIP YQPNGTVEYL IAAIVPEEHE FEKEFQLTSA IKKELAASLP AYMIPRKFIY 

       490        500 
QDHIQMTANG KIDRKRIGEE VLV

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees."
Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.
Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation."
Perego M., Glaser P., Minutello A., Strauch M.A., Leopold K., Fischer W.
J. Biol. Chem. 270:15598-15606(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X73124 Genomic DNA. Translation: CAA51561.1.
AL009126 Genomic DNA. Translation: CAB15876.1.
PIRS39660.
RefSeqNP_391729.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E7WX-ray2.28A1-503[»]
3E7XX-ray2.60A1-503[»]
ProteinModelPortalP39581.
SMRP39581. Positions 1-503.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU38500.

Proteomic databases

PaxDbP39581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15876; CAB15876; BSU38500.
GeneID937358.
KEGGbsu:BSU38500.
PATRIC18979748. VBIBacSub10457_4036.

Organism-specific databases

GenoListBSU38500. [Micado]

Phylogenomic databases

eggNOGCOG1020.
HOGENOMHOG000229995.
KOK03367.
OMAHIQMTAN.
ProtClustDBPRK04813.

Enzyme and pathway databases

BioCycBSUB:BSU38500-MONOMER.
UniPathwayUPA00556.

Family and domain databases

HAMAPMF_00593. DltA.
InterProIPR010071. AA_adenyl_domain.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. D_ala_DACP_lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP39581.

Entry information

Entry nameDLTA_BACSU
AccessionPrimary (citable) accession number: P39581
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents