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Protein

D-alanine--D-alanyl carrier protein ligase

Gene

dltA

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.UniRule annotation1 Publication

Catalytic activityi

D-alanine + ATP + holo-[D-alanyl-carrier protein] = AMP + diphosphate + D-alanyl-[D-alanyl-carrier protein].UniRule annotation1 Publication

Kineticsi

  1. KM=1.1 mM for D-alanine1 Publication
  2. KM=14.4 mM for L-alanine1 Publication

    Pathwayi: lipoteichoic acid biosynthesis

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei197D-alanineUniRule annotationCombined sources1 Publication1
    Binding sitei301D-alanine; via carbonyl oxygenUniRule annotationCombined sources1 Publication1
    Binding sitei383ATPUniRule annotationCombined sources2 Publications1
    Binding sitei492ATPUniRule annotationCombined sources2 Publications1
    Binding sitei492D-alanineUniRule annotationCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi152 – 153ATPUniRule annotationCombined sources1 Publication2
    Nucleotide bindingi292 – 297ATPUniRule annotationCombined sources2 Publications6
    Nucleotide bindingi394 – 397ATPUniRule annotationCombined sources2 Publications4

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLigase
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.13 648
    UniPathwayiUPA00556

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-alanine--D-alanyl carrier protein ligaseUniRule annotation (EC:6.2.1.-UniRule annotation1 Publication)
    Short name:
    DCLUniRule annotation
    Alternative name(s):
    D-alanine--poly(phosphoribitol) ligase subunit 1UniRule annotation
    D-alanine-activating enzymeUniRule annotation
    Short name:
    DAEUniRule annotation
    Gene namesi
    Name:dltAUniRule annotation
    Ordered Locus Names:BC_1372
    OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
    Taxonomic identifieri226900 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    Proteomesi
    • UP000001417 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi269C → A: Relaxes D-alanine preference, allowing the enzyme to use L-alanine at the same efficiency. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_10000255261 – 504D-alanine--D-alanyl carrier protein ligaseAdd BLAST504

    Interactioni

    Protein-protein interaction databases

    STRINGi226900.BC1372

    Structurei

    Secondary structure

    1504
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 13Combined sources11
    Beta strandi17 – 22Combined sources6
    Beta strandi25 – 28Combined sources4
    Helixi29 – 46Combined sources18
    Beta strandi54 – 60Combined sources7
    Helixi62 – 73Combined sources12
    Beta strandi78 – 82Combined sources5
    Helixi87 – 96Combined sources10
    Beta strandi101 – 106Combined sources6
    Beta strandi114 – 119Combined sources6
    Helixi121 – 129Combined sources9
    Turni130 – 132Combined sources3
    Helixi137 – 139Combined sources3
    Beta strandi145 – 152Combined sources8
    Beta strandi160 – 165Combined sources6
    Helixi166 – 179Combined sources14
    Beta strandi187 – 190Combined sources4
    Helixi197 – 199Combined sources3
    Helixi200 – 208Combined sources9
    Beta strandi212 – 215Combined sources4
    Helixi218 – 222Combined sources5
    Helixi224 – 234Combined sources11
    Beta strandi238 – 241Combined sources4
    Helixi243 – 249Combined sources7
    Turni257 – 259Combined sources3
    Beta strandi265 – 268Combined sources4
    Helixi275 – 284Combined sources10
    Beta strandi289 – 294Combined sources6
    Helixi297 – 299Combined sources3
    Beta strandi303 – 307Combined sources5
    Helixi310 – 315Combined sources6
    Beta strandi322 – 324Combined sources3
    Beta strandi329 – 333Combined sources5
    Beta strandi335 – 337Combined sources3
    Beta strandi346 – 352Combined sources7
    Helixi363 – 369Combined sources7
    Beta strandi370 – 373Combined sources4
    Beta strandi376 – 388Combined sources13
    Beta strandi391 – 397Combined sources7
    Helixi398 – 400Combined sources3
    Beta strandi402 – 404Combined sources3
    Beta strandi407 – 409Combined sources3
    Helixi411 – 420Combined sources10
    Beta strandi424 – 434Combined sources11
    Beta strandi437 – 447Combined sources11
    Helixi455 – 467Combined sources13
    Helixi472 – 474Combined sources3
    Beta strandi477 – 481Combined sources5
    Beta strandi491 – 493Combined sources3
    Helixi495 – 503Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3DHVX-ray2.00A1-504[»]
    3FCCX-ray2.32A1-504[»]
    3FCEX-ray1.90A1-504[»]
    4PZPX-ray1.90A2-504[»]
    ProteinModelPortaliQ81G39
    SMRiQ81G39
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ81G39

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4108IQD Bacteria
    COG1020 LUCA
    KOiK03367
    OMAiNFYIIFT

    Family and domain databases

    HAMAPiMF_00593 DltA, 1 hit
    InterProiView protein in InterPro
    IPR010071 AA_adenyl_domain
    IPR025110 AMP-bd_C
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR010072 DltA
    PfamiView protein in Pfam
    PF00501 AMP-binding, 1 hit
    PF13193 AMP-binding_C, 1 hit
    TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
    TIGR01734 D-ala-DACP-lig, 1 hit
    PROSITEiView protein in PROSITE
    PS00455 AMP_BINDING, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q81G39-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLLEQIEKW AAETPDQTAF VWRDAKITYK QLKEDSDALA HWISSEYPDD
    60 70 80 90 100
    RSPIMVYGHM QPEMIINFLG CVKAGHAYIP VDLSIPADRV QRIAENSGAK
    110 120 130 140 150
    LLLSATAVTV TDLPVRIVSE DNLKDIFFTH KGNTPNPEHA VKGDENFYII
    160 170 180 190 200
    YTSGSTGNPK GVQITYNCLV SFTKWAVEDF NLQTGQVFLN QAPFSFDLSV
    210 220 230 240 250
    MDIYPSLVTG GTLWAIDKDM IARPKDLFAS LEQSDIQVWT STPSFAEMCL
    260 270 280 290 300
    MEASFSESML PNMKTFLFCG EVLPNEVARK LIERFPKATI MNTYGPTEAT
    310 320 330 340 350
    VAVTGIHVTE EVLDQYKSLP VGYCKSDCRL LIMKEDGTIA PDGEKGEIVI
    360 370 380 390 400
    VGPSVSVGYL GSPELTEKAF TMIDGERAYK TGDAGYVENG LLFYNGRLDF
    410 420 430 440 450
    QIKLHGYRME LEEIEHHLRA CSYVEGAVIV PIKKGEKYDY LLAVVVPGEH
    460 470 480 490 500
    SFEKEFKLTS AIKKELNERL PNYMIPRKFM YQSSIPMTPN GKVDRKKLLS

    EVTA
    Length:504
    Mass (Da):56,494
    Last modified:June 1, 2003 - v1
    Checksum:i96BE762A25E315D2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016877 Genomic DNA Translation: AAP08354.1
    RefSeqiNP_831153.1, NC_004722.1
    WP_000770505.1, NC_004722.1

    Genome annotation databases

    EnsemblBacteriaiAAP08354; AAP08354; BC_1372
    GeneIDi1203721
    KEGGibce:BC1372
    PATRICifig|226900.8.peg.1346

    Similar proteinsi

    Entry informationi

    Entry nameiDLTA_BACCR
    AccessioniPrimary (citable) accession number: Q81G39
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 1, 2003
    Last modified: May 23, 2018
    This is version 89 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

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