Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q11GS0

- MURE_CHESB

UniProt

Q11GS0 - MURE_CHESB

Protein

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

Gene

murE

Organism
Chelativorans sp. (strain BNC1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei29 – 291UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei176 – 1761UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei182 – 1821UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei184 – 1841UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei380 – 3801Meso-diaminopimelateUniRule annotation
    Binding sitei452 – 4521Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
    Binding sitei456 – 4561Meso-diaminopimelateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi107 – 1137ATPUniRule 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

    BioCyciCSP266779:GI09-2046-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:Meso_2012
    OrganismiChelativorans sp. (strain BNC1)
    Taxonomic identifieri266779 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans
    ProteomesiUP000001820: 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 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_1000012372Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei216 – 2161N6-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

    STRINGi266779.Meso_2012.

    Structurei

    3D structure databases

    ProteinModelPortaliQ11GS0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni149 – 1502UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni404 – 4074Meso-diaminopimelate bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi404 – 4074Meso-diaminopimelate recognition motif

    Sequence similaritiesi

    Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0769.
    HOGENOMiHOG000268118.
    KOiK01928.
    OMAiKIAVDYA.
    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.

    Q11GS0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLGEFADIL PLSGSIAGET TISGLASDSR RVNAGDLFFA LQGSKADGAA    50
    YAADAAGRGA VAIIARPGTV GDVGVPVIEA DDPRHVLALA SARLYGAQPA 100
    TMVAVTGTSG KTSVAAFTRQ IWEKAGLAAA SIGTTGVVAP GRDEYGELTT 150
    PDPVSLHKLL RELADAGVTH ASMEASSHGL DQRRLDGVKL AAGGFTNLGR 200
    DHMDYHPTVE HYHQSKMRLF KTLLPKGAPA VIFADDPWSE PTEKVALAAG 250
    LQLLTVGRRG TFLTIKRVEH ERHRQRTEIE HEGMIYDIML PLAGDFQVGN 300
    ALVAAGLAIS TGLPADKAVA ALEHLKGASG RLELTGTTED GAQIYVDYAH 350
    KPDALENVLQ AVRPFTTGRV IVVFGCGGDR DPGKRPIMGE IARRLADVVI 400
    VTDDNPRSEV PAEIRRAILE AVPEATEIGD RREAIRTAVA MLNSGDTLIV 450
    AGKGHEIGQE IAGTKLPFSD HEEVRRALKE RTA 483
    Length:483
    Mass (Da):51,101
    Last modified:August 22, 2006 - v1
    Checksum:iA34DDB6E426467D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000390 Genomic DNA. Translation: ABG63405.1.
    RefSeqiWP_011581347.1. NC_008254.1.
    YP_674570.1. NC_008254.1.

    Genome annotation databases

    EnsemblBacteriaiABG63405; ABG63405; Meso_2012.
    GeneIDi4182805.
    KEGGimes:Meso_2012.
    PATRICi21344130. VBICheSp72577_2687.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000390 Genomic DNA. Translation: ABG63405.1 .
    RefSeqi WP_011581347.1. NC_008254.1.
    YP_674570.1. NC_008254.1.

    3D structure databases

    ProteinModelPortali Q11GS0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266779.Meso_2012.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG63405 ; ABG63405 ; Meso_2012 .
    GeneIDi 4182805.
    KEGGi mes:Meso_2012.
    PATRICi 21344130. VBICheSp72577_2687.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci CSP266779:GI09-2046-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BNC1.

    Entry informationi

    Entry nameiMURE_CHESB
    AccessioniPrimary (citable) accession number: Q11GS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 66 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, Reference proteome

    Documents

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

    External Data

    Dasty 3