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Q9ZJC6

- MURE_HELPJ

UniProt

Q9ZJC6 - MURE_HELPJ

Protein

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

Gene

murE

Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.UniRule annotation

    Catalytic activityi

    ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei144 – 1441UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei150 – 1501UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei152 – 1521UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei340 – 3401Meso-diaminopimelateUniRule annotation
    Binding sitei415 – 4151Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
    Binding sitei419 – 4191Meso-diaminopimelateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi74 – 807ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. tetrahydrofolylpolyglutamate synthase activity Source: InterPro
    3. UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
    4. regulation of cell shape Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciHPYL85963:GJB9-1426-MONOMER.
    UniPathwayiUPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseUniRule annotation (EC:6.3.2.13UniRule annotation)
    Alternative name(s):
    Meso-A2pm-adding enzymeUniRule annotation
    Meso-diaminopimelate-adding enzymeUniRule annotation
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligaseUniRule annotation
    UDP-MurNAc-tripeptide synthetaseUniRule annotation
    UDP-N-acetylmuramyl-tripeptide synthetaseUniRule annotation
    Gene namesi
    Name:murEUniRule annotation
    Ordered Locus Names:jhp_1387
    OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
    Taxonomic identifieri85963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    ProteomesiUP000000804: 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 – 447447UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101903Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei184 – 1841N6-carboxylysineUniRule annotation

    Post-translational modificationi

    Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.UniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi85963.jhp1387.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZJC6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni117 – 1182UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni364 – 3674Meso-diaminopimelate bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi364 – 3674Meso-diaminopimelate recognition motif

    Sequence similaritiesi

    Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0769.
    KOiK01928.
    OMAiAVMTNLS.
    OrthoDBiEOG6PKFCR.

    Family and domain databases

    Gene3Di3.40.1190.10. 1 hit.
    3.90.190.20. 1 hit.
    HAMAPiMF_00208. MurE.
    InterProiIPR018109. Folylpolyglutamate_synth_CS.
    IPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
    [Graphical view]
    PfamiPF02875. Mur_ligase_C. 1 hit.
    PF08245. Mur_ligase_M. 1 hit.
    [Graphical view]
    SUPFAMiSSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    TIGRFAMsiTIGR01085. murE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9ZJC6-1 [UniParc]FASTAAdd to Basket

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    MKLKKTLTYQ HHAYSFLSDN TNEVLENPKE ILFVKTPLNE KYAPLIAEKN    50
    LAILDFNELK NYFDFKIKIV GITGTNGKTT TASLMYSLLL DLNKKTALLG 100
    TRGFFIDDKH IKEKGLTTPT LLELYSDLEE AIRLKCEYFI MEVSSHAIVQ 150
    KRIAGLDFAL KILTNITSDH LDFHQNIENY RDAKNSFFKD EGLKVINRDE 200
    TNALFNPINA RTYALDKKAH LNVQAFSLNP SISASLCYQH DLRDPNLKET 250
    ALIHSPLLGR YNLYNILAGV LGVKLLTQLP LETIAPLLEN FYGVKGRLEI 300
    VHSKPLVVVD FAHTTDGMQQ VFESFKNQKI TALFGAGGDR DKTKRPKMGA 350
    IASCYAHQII LTSDNPRSEN EEDIIKDILK GINNSSKVIV EKDRKKAILN 400
    ALENLKDDEV LLILGKGDEN IQIFKDKTIF FSDQEVVKDY YLNLKQG 447
    Length:447
    Mass (Da):50,660
    Last modified:May 1, 1999 - v1
    Checksum:i639AB9D18F3740BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001439 Genomic DNA. Translation: AAD06968.1.
    PIRiD71812.
    RefSeqiNP_224105.1. NC_000921.1.

    Genome annotation databases

    EnsemblBacteriaiAAD06968; AAD06968; jhp_1387.
    GeneIDi889938.
    KEGGihpj:jhp1387.
    PATRICi20607654. VBIHelPyl98156_1506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001439 Genomic DNA. Translation: AAD06968.1 .
    PIRi D71812.
    RefSeqi NP_224105.1. NC_000921.1.

    3D structure databases

    ProteinModelPortali Q9ZJC6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 85963.jhp1387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD06968 ; AAD06968 ; jhp_1387 .
    GeneIDi 889938.
    KEGGi hpj:jhp1387.
    PATRICi 20607654. VBIHelPyl98156_1506.

    Phylogenomic databases

    eggNOGi COG0769.
    KOi K01928.
    OMAi AVMTNLS.
    OrthoDBi EOG6PKFCR.

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci HPYL85963:GJB9-1426-MONOMER.

    Family and domain databases

    Gene3Di 3.40.1190.10. 1 hit.
    3.90.190.20. 1 hit.
    HAMAPi MF_00208. MurE.
    InterProi IPR018109. Folylpolyglutamate_synth_CS.
    IPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
    [Graphical view ]
    Pfami PF02875. Mur_ligase_C. 1 hit.
    PF08245. Mur_ligase_M. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    TIGRFAMsi TIGR01085. murE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: J99 / ATCC 700824.

    Entry informationi

    Entry nameiMURE_HELPJ
    AccessioniPrimary (citable) accession number: Q9ZJC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 105 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

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3