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Protein

D-alanine--poly(phosphoribitol) ligase subunit 1

Gene

dltA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D-alanyl-poly(ribitol phosphate).UniRule annotation

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. D-alanine-poly(phosphoribitol) ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipoteichoic acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU38500-MONOMER.
SABIO-RKP39581.
UniPathwayiUPA00556.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanine--poly(phosphoribitol) ligase subunit 1UniRule annotation (EC:6.1.1.13UniRule annotation)
Alternative name(s):
D-alanine-D-alanyl carrier protein ligaseUniRule annotation
Short name:
DCLUniRule annotation
D-alanine-activating enzymeUniRule annotation
Short name:
DAEUniRule annotation
Gene namesi
Name:dltAUniRule annotation
Synonyms:dae
Ordered Locus Names:BSU38500
ORF Names:ipa-5r
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU38500. [Micado]

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503D-alanine--poly(phosphoribitol) ligase subunit 1PRO_0000213142Add
BLAST

Proteomic databases

PaxDbiP39581.

Interactioni

Protein-protein interaction databases

IntActiP39581. 1 interaction.
MINTiMINT-8366705.
STRINGi224308.BSU38500.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311Combined sources
Beta strandi17 – 226Combined sources
Beta strandi25 – 284Combined sources
Helixi29 – 4315Combined sources
Turni44 – 463Combined sources
Beta strandi49 – 513Combined sources
Beta strandi55 – 617Combined sources
Helixi63 – 7513Combined sources
Beta strandi79 – 835Combined sources
Helixi88 – 9811Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi120 – 1223Combined sources
Helixi123 – 1275Combined sources
Helixi136 – 1383Combined sources
Beta strandi144 – 1518Combined sources
Beta strandi159 – 1646Combined sources
Helixi165 – 17814Combined sources
Turni180 – 1845Combined sources
Beta strandi186 – 1894Combined sources
Helixi197 – 20711Combined sources
Beta strandi211 – 2144Combined sources
Helixi217 – 2215Combined sources
Helixi223 – 23311Combined sources
Beta strandi236 – 2405Combined sources
Helixi242 – 2498Combined sources
Turni256 – 2583Combined sources
Beta strandi264 – 2674Combined sources
Helixi274 – 28310Combined sources
Beta strandi288 – 2914Combined sources
Helixi296 – 2983Combined sources
Beta strandi302 – 3076Combined sources
Helixi309 – 3124Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi328 – 3325Combined sources
Beta strandi345 – 3517Combined sources
Helixi362 – 3687Combined sources
Beta strandi369 – 38719Combined sources
Beta strandi390 – 40314Combined sources
Beta strandi406 – 4094Combined sources
Helixi410 – 41910Combined sources
Beta strandi423 – 4319Combined sources
Beta strandi433 – 4364Combined sources
Beta strandi439 – 4468Combined sources
Helixi454 – 46815Combined sources
Helixi471 – 4733Combined sources
Beta strandi476 – 4805Combined sources
Helixi488 – 4903Combined sources
Helixi494 – 50310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E7WX-ray2.28A1-503[»]
3E7XX-ray2.60A1-503[»]
ProteinModelPortaliP39581.
SMRiP39581. Positions 1-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39581.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1020.
HOGENOMiHOG000229995.
InParanoidiP39581.
KOiK03367.
OMAiLDTHART.
OrthoDBiEOG6QP0WP.
PhylomeDBiP39581.

Family and domain databases

HAMAPiMF_00593. DltA.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. DltA.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39581-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLHAIQTH AETYPQTDAF RSQGQSLTYQ ELWEQSDRAA AAIQKRISGE
60 70 80 90 100
KKSPILVYGH MEPHMIVSFL GSVKAGHPYI PVDLSIPSER IAKIIESSGA
110 120 130 140 150
ELLIHAAGLS IDAVGQQIQT VSAEELLENE GGSVSQDQWV KEHETFYIIY
160 170 180 190 200
TSGSTGNPKG VQISAANLQS FTDWICADFP VSGGKIFLNQ APFSFDLSVM
210 220 230 240 250
DLYPCLQSGG TLHCVTKDAV NKPKVLFEEL KKSGLNVWTS TPSFVQMCLM
260 270 280 290 300
DPGFSQDLLP HADTFMFCGE VLPVSVAKAL LERFPKAKIF NTYGPTEATV
310 320 330 340 350
AVTSVEITND VISRSESLPV GFAKPDMNIF IMDEEGQPLP EGEKGEIVIA
360 370 380 390 400
GPSVSRGYLG EPELTEKAFF SHEGQWAYRT GDAGFIQDGQ IFCQGRLDFQ
410 420 430 440 450
IKLHGYRMEL EEIEFHVRQS QYVRSAVVIP YQPNGTVEYL IAAIVPEEHE
460 470 480 490 500
FEKEFQLTSA IKKELAASLP AYMIPRKFIY QDHIQMTANG KIDRKRIGEE

VLV
Length:503
Mass (Da):55,809
Last modified:February 1, 1995 - v1
Checksum:i76604AA90C812644
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51561.1.
AL009126 Genomic DNA. Translation: CAB15876.1.
PIRiS39660.
RefSeqiNP_391729.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15876; CAB15876; BSU38500.
GeneIDi937358.
KEGGibsu:BSU38500.
PATRICi18979748. VBIBacSub10457_4036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51561.1.
AL009126 Genomic DNA. Translation: CAB15876.1.
PIRiS39660.
RefSeqiNP_391729.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E7WX-ray2.28A1-503[»]
3E7XX-ray2.60A1-503[»]
ProteinModelPortaliP39581.
SMRiP39581. Positions 1-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39581. 1 interaction.
MINTiMINT-8366705.
STRINGi224308.BSU38500.

Proteomic databases

PaxDbiP39581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15876; CAB15876; BSU38500.
GeneIDi937358.
KEGGibsu:BSU38500.
PATRICi18979748. VBIBacSub10457_4036.

Organism-specific databases

GenoListiBSU38500. [Micado]

Phylogenomic databases

eggNOGiCOG1020.
HOGENOMiHOG000229995.
InParanoidiP39581.
KOiK03367.
OMAiLDTHART.
OrthoDBiEOG6QP0WP.
PhylomeDBiP39581.

Enzyme and pathway databases

UniPathwayiUPA00556.
BioCyciBSUB:BSU38500-MONOMER.
SABIO-RKP39581.

Miscellaneous databases

EvolutionaryTraceiP39581.

Family and domain databases

HAMAPiMF_00593. DltA.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR010072. DltA.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
TIGR01734. D-ala-DACP-lig. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.

Entry informationi

Entry nameiDLTA_BACSU
AccessioniPrimary (citable) accession number: P39581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.