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P39581

- DLTA_BACSU

UniProt

P39581 - DLTA_BACSU

Protein

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

Gene

dltA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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. AMP binding Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. D-alanine-poly(phosphoribitol) ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipoteichoic acid biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU38500-MONOMER.
    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK03367.
    OMAiPLVCIEK.
    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

    MKLLHAIQTH AETYPQTDAF RSQGQSLTYQ ELWEQSDRAA AAIQKRISGE    50
    KKSPILVYGH MEPHMIVSFL GSVKAGHPYI PVDLSIPSER IAKIIESSGA 100
    ELLIHAAGLS IDAVGQQIQT VSAEELLENE GGSVSQDQWV KEHETFYIIY 150
    TSGSTGNPKG VQISAANLQS FTDWICADFP VSGGKIFLNQ APFSFDLSVM 200
    DLYPCLQSGG TLHCVTKDAV NKPKVLFEEL KKSGLNVWTS TPSFVQMCLM 250
    DPGFSQDLLP HADTFMFCGE VLPVSVAKAL LERFPKAKIF NTYGPTEATV 300
    AVTSVEITND VISRSESLPV GFAKPDMNIF IMDEEGQPLP EGEKGEIVIA 350
    GPSVSRGYLG EPELTEKAFF SHEGQWAYRT GDAGFIQDGQ IFCQGRLDFQ 400
    IKLHGYRMEL EEIEFHVRQS QYVRSAVVIP YQPNGTVEYL IAAIVPEEHE 450
    FEKEFQLTSA IKKELAASLP AYMIPRKFIY QDHIQMTANG KIDRKRIGEE 500
    VLV 503
    Length:503
    Mass (Da):55,809
    Last modified:February 1, 1995 - v1
    Checksum:i76604AA90C812644
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73124 Genomic DNA. Translation: CAA51561.1 .
    AL009126 Genomic DNA. Translation: CAB15876.1 .
    PIRi S39660.
    RefSeqi NP_391729.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E7W X-ray 2.28 A 1-503 [» ]
    3E7X X-ray 2.60 A 1-503 [» ]
    ProteinModelPortali P39581.
    SMRi P39581. Positions 1-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P39581. 1 interaction.
    MINTi MINT-8366705.
    STRINGi 224308.BSU38500.

    Proteomic databases

    PaxDbi P39581.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15876 ; CAB15876 ; BSU38500 .
    GeneIDi 937358.
    KEGGi bsu:BSU38500.
    PATRICi 18979748. VBIBacSub10457_4036.

    Organism-specific databases

    GenoListi BSU38500. [Micado ]

    Phylogenomic databases

    eggNOGi COG1020.
    HOGENOMi HOG000229995.
    KOi K03367.
    OMAi PLVCIEK.
    OrthoDBi EOG6QP0WP.
    PhylomeDBi P39581.

    Enzyme and pathway databases

    UniPathwayi UPA00556 .
    BioCyci BSUB:BSU38500-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39581.

    Family and domain databases

    HAMAPi MF_00593. DltA.
    InterProi IPR010071. AA_adenyl_domain.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR010072. DltA.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
    TIGR01734. D-ala-DACP-lig. 1 hit.
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 104 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