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Q81G39

- DLTA_BACCR

UniProt

Q81G39 - DLTA_BACCR

Protein

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

Gene

dltA

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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.UniRule annotation

    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

    BioCyciBCER226900:GJEU-1372-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
    Ordered Locus Names:BC_1372
    OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)
    Taxonomic identifieri226900 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000001417: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 504504D-alanine--poly(phosphoribitol) ligase subunit 1PRO_1000025526Add
    BLAST

    Proteomic databases

    PRIDEiQ81G39.

    Interactioni

    Protein-protein interaction databases

    STRINGi226900.BC1372.

    Structurei

    Secondary structure

    1
    504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Beta strandi17 – 226
    Beta strandi25 – 284
    Helixi29 – 4618
    Beta strandi54 – 607
    Helixi62 – 7312
    Beta strandi78 – 825
    Helixi87 – 9610
    Beta strandi101 – 1066
    Beta strandi114 – 1196
    Helixi121 – 1299
    Turni130 – 1323
    Helixi137 – 1393
    Beta strandi145 – 1528
    Beta strandi160 – 1656
    Helixi166 – 17914
    Beta strandi187 – 1904
    Helixi197 – 1993
    Helixi200 – 2089
    Beta strandi212 – 2154
    Helixi218 – 2225
    Helixi224 – 23411
    Beta strandi238 – 2414
    Helixi243 – 2497
    Turni257 – 2593
    Beta strandi265 – 2684
    Helixi275 – 28410
    Beta strandi289 – 2946
    Helixi297 – 2993
    Beta strandi303 – 3075
    Helixi310 – 3156
    Beta strandi322 – 3243
    Beta strandi329 – 3335
    Beta strandi335 – 3373
    Beta strandi346 – 3527
    Helixi363 – 3697
    Beta strandi370 – 3734
    Beta strandi376 – 38813
    Beta strandi391 – 3977
    Helixi398 – 4003
    Beta strandi402 – 4043
    Beta strandi407 – 4093
    Helixi411 – 42010
    Beta strandi424 – 43411
    Beta strandi437 – 44711
    Helixi455 – 46713
    Helixi472 – 4743
    Beta strandi477 – 4815
    Beta strandi491 – 4933
    Helixi495 – 5039

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DHVX-ray2.00A1-504[»]
    3FCCX-ray2.32A1-504[»]
    3FCEX-ray1.90A1-504[»]
    ProteinModelPortaliQ81G39.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ81G39.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1020.
    KOiK03367.
    OMAiIANQAPF.
    OrthoDBiEOG6QP0WP.

    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.

    Q81G39-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLEQIEKW AAETPDQTAF VWRDAKITYK QLKEDSDALA HWISSEYPDD    50
    RSPIMVYGHM QPEMIINFLG CVKAGHAYIP VDLSIPADRV QRIAENSGAK 100
    LLLSATAVTV TDLPVRIVSE DNLKDIFFTH KGNTPNPEHA VKGDENFYII 150
    YTSGSTGNPK GVQITYNCLV SFTKWAVEDF NLQTGQVFLN QAPFSFDLSV 200
    MDIYPSLVTG GTLWAIDKDM IARPKDLFAS LEQSDIQVWT STPSFAEMCL 250
    MEASFSESML PNMKTFLFCG EVLPNEVARK LIERFPKATI MNTYGPTEAT 300
    VAVTGIHVTE EVLDQYKSLP VGYCKSDCRL LIMKEDGTIA PDGEKGEIVI 350
    VGPSVSVGYL GSPELTEKAF TMIDGERAYK TGDAGYVENG LLFYNGRLDF 400
    QIKLHGYRME LEEIEHHLRA CSYVEGAVIV PIKKGEKYDY LLAVVVPGEH 450
    SFEKEFKLTS AIKKELNERL PNYMIPRKFM YQSSIPMTPN GKVDRKKLLS 500
    EVTA 504
    Length:504
    Mass (Da):56,494
    Last modified:June 1, 2003 - v1
    Checksum:i96BE762A25E315D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016877 Genomic DNA. Translation: AAP08354.1.
    RefSeqiNP_831153.1. NC_004722.1.

    Genome annotation databases

    EnsemblBacteriaiAAP08354; AAP08354; BC_1372.
    GeneIDi1203721.
    KEGGibce:BC1372.
    PATRICi32598473. VBIBacCer54481_1346.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016877 Genomic DNA. Translation: AAP08354.1 .
    RefSeqi NP_831153.1. NC_004722.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DHV X-ray 2.00 A 1-504 [» ]
    3FCC X-ray 2.32 A 1-504 [» ]
    3FCE X-ray 1.90 A 1-504 [» ]
    ProteinModelPortali Q81G39.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226900.BC1372.

    Proteomic databases

    PRIDEi Q81G39.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP08354 ; AAP08354 ; BC_1372 .
    GeneIDi 1203721.
    KEGGi bce:BC1372.
    PATRICi 32598473. VBIBacCer54481_1346.

    Phylogenomic databases

    eggNOGi COG1020.
    KOi K03367.
    OMAi IANQAPF.
    OrthoDBi EOG6QP0WP.

    Enzyme and pathway databases

    UniPathwayi UPA00556 .
    BioCyci BCER226900:GJEU-1372-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q81G39.

    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 [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 14579 / DSM 31.

    Entry informationi

    Entry nameiDLTA_BACCR
    AccessioniPrimary (citable) accession number: Q81G39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 75 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. 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

    External Data

    Dasty 3