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Q83MG0

- MURE_SHIFL

UniProt

Q83MG0 - MURE_SHIFL

Protein

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

Gene

murE

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei27 – 271UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygenUniRule annotation
    Binding sitei29 – 291UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei157 – 1571UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei185 – 1851UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei191 – 1911UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei193 – 1931UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei390 – 3901Meso-diaminopimelateUniRule annotation
    Binding sitei465 – 4651Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
    Binding sitei469 – 4691Meso-diaminopimelateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi116 – 1227ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. 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

    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:SF0082, S0084
    OrganismiShigella flexneri
    Taxonomic identifieri623 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000001006: Chromosome, UP000002673: 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 – 495495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101939Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei225 – 2251N6-carboxylysineUniRule annotation

    Post-translational modificationi

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

    Proteomic databases

    PaxDbiQ83MG0.

    Interactioni

    Protein-protein interaction databases

    STRINGi198214.SF0082.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83MG0.
    SMRiQ83MG0. Positions 3-495.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 463UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni158 – 1592UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni414 – 4174Meso-diaminopimelate bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi414 – 4174Meso-diaminopimelate recognition motif

    Sequence similaritiesi

    Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0769.
    HOGENOMiHOG000268118.
    KOiK01928.
    OMAiAVMTNLS.
    OrthoDBiEOG6PKFCR.

    Family and domain databases

    Gene3Di3.40.1190.10. 1 hit.
    3.40.1390.10. 1 hit.
    3.90.190.20. 1 hit.
    HAMAPiMF_00208. MurE.
    InterProiIPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    IPR000713. Mur_ligase_N.
    IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
    [Graphical view]
    PfamiPF01225. Mur_ligase. 1 hit.
    PF02875. Mur_ligase_C. 1 hit.
    PF08245. Mur_ligase_M. 1 hit.
    [Graphical view]
    SUPFAMiSSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    SSF63418. SSF63418. 1 hit.
    TIGRFAMsiTIGR01085. murE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q83MG0-1 [UniParc]FASTAAdd to Basket

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    MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR    50
    YIPQAIAQGV AAIIAEAKDE ATDGEIREMH GVPVIYLSQL NERLSALAGR 100
    FYHEPSDNLR LVGVTGTNGK TTTTQLLAQW SQLLGETSAV MGTVGNGLLG 150
    KVIPTENTTG SAVDVQHELA GLVDQGATFC AMEVSSHGLV QHRVAALKFP 200
    ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN ADDEVGRRWL 250
    AKLPDAVAVS MEDHINPNCH GRWLKATEVN YHDSGATIRF SSSWGDGEIE 300
    SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG 350
    KPTVVVDYAH TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA 400
    IAEEFADVAV VTDDNPRTEE PRAIINDILA GMLDAGHAKV MEGRAEAVTC 450
    AVMQAKENDV VLVAGKGHED YQIVGNQRLD YSDRVTVARL LGGIA 495
    Length:495
    Mass (Da):53,315
    Last modified:June 1, 2003 - v1
    Checksum:iF070E7ECF0907A9C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN41747.1.
    AE014073 Genomic DNA. Translation: AAP15628.1.
    RefSeqiNP_706040.1. NC_004337.2.
    NP_835823.1. NC_004741.1.

    Genome annotation databases

    EnsemblBacteriaiAAN41747; AAN41747; SF0082.
    AAP15628; AAP15628; S0084.
    GeneIDi1024503.
    1076514.
    KEGGisfl:SF0082.
    sfx:S0084.
    PATRICi18701108. VBIShiFle31049_0096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN41747.1 .
    AE014073 Genomic DNA. Translation: AAP15628.1 .
    RefSeqi NP_706040.1. NC_004337.2.
    NP_835823.1. NC_004741.1.

    3D structure databases

    ProteinModelPortali Q83MG0.
    SMRi Q83MG0. Positions 3-495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198214.SF0082.

    Proteomic databases

    PaxDbi Q83MG0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN41747 ; AAN41747 ; SF0082 .
    AAP15628 ; AAP15628 ; S0084 .
    GeneIDi 1024503.
    1076514.
    KEGGi sfl:SF0082.
    sfx:S0084.
    PATRICi 18701108. VBIShiFle31049_0096.

    Phylogenomic databases

    eggNOGi COG0769.
    HOGENOMi HOG000268118.
    KOi K01928.
    OMAi AVMTNLS.
    OrthoDBi EOG6PKFCR.

    Enzyme and pathway databases

    UniPathwayi UPA00219 .

    Family and domain databases

    Gene3Di 3.40.1190.10. 1 hit.
    3.40.1390.10. 1 hit.
    3.90.190.20. 1 hit.
    HAMAPi MF_00208. MurE.
    InterProi IPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    IPR000713. Mur_ligase_N.
    IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
    [Graphical view ]
    Pfami PF01225. Mur_ligase. 1 hit.
    PF02875. Mur_ligase_C. 1 hit.
    PF08245. Mur_ligase_M. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    SSF63418. SSF63418. 1 hit.
    TIGRFAMsi TIGR01085. murE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
      Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
      , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
      Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 301 / Serotype 2a.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700930 / 2457T / Serotype 2a.

    Entry informationi

    Entry nameiMURE_SHIFL
    AccessioniPrimary (citable) accession number: Q83MG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 85 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