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O26027

- MURE_HELPY

UniProt

O26027 - MURE_HELPY

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Protein

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

Gene
murE, HP_1494
Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 By similarity.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-Glu By similarity
Binding sitei144 – 1441UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei150 – 1501UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei152 – 1521UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei340 – 3401Meso-diaminopimelate By similarity
Binding sitei415 – 4151Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding sitei419 – 4191Meso-diaminopimelate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 807ATP Reviewed prediction

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
Complete GO annotation...

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

BioCyciHPY:HP1494-MONOMER.
UniPathwayiUPA00219.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC:6.3.2.13)
Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
Gene namesi
Name:murE
Ordered Locus Names:HP_1494
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 ligaseUniRule annotationPRO_0000101902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841N6-carboxylysine By similarity

Post-translational modificationi

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

Proteomic databases

PRIDEiO26027.

Interactioni

Protein-protein interaction databases

IntActiO26027. 1 interaction.
STRINGi85962.HP1494.

Structurei

3D structure databases

ProteinModelPortaliO26027.

Family & Domainsi

Region

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

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0769.
KOiK01928.
OMAiGMIASEW.
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.

O26027-1 [UniParc]FASTAAdd to Basket

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MKLKKTLTYQ NHTYSFLSDN THEVLENPKE ILFVKTPLNE KYSHLIAEKN    50
LAILDFNELK NYFDFKIKIV GITGTNGKTT TASLMYSLLL DLNKKTALLG 100
TRGFFINNER IKEKGLTTPT LLELYSDLEE AVRLKCEYFI MEVSSHAIVQ 150
KRIAGLDFAL KILTNITSDH LDFHQSIENY RDAKNSFFKD EGLKVINRDE 200
TNALFNPVNA HTYALDKKAH LNVQAFSLNP SISASLCYQQ DLRDPNFKEI 250
ALMHSPLLGR YNLYNILAGV LGVKLLTQLP LETIVPLLEN FYGVKGRLEI 300
VHSKPLVVVD FAHTIDGMQQ VFESFKNQKI TALFGAGGDR DKTKRPEMGA 350
IASYYAHKII LTSDNPRSEN EEDIIKDILK GINDSSKVIV EKDRKKAILN 400
ALENLKDDEV LLILGKGDEN IQIFKDKTIF FSDQEVVKSY YQHLKQG 447
Length:447
Mass (Da):50,858
Last modified:January 1, 1998 - v1
Checksum:i296349E8FE90AD34
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD08535.1.
PIRiF64706.
RefSeqiNP_208285.1. NC_000915.1.
YP_006935420.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08535; AAD08535; HP_1494.
GeneIDi13870710.
899798.
KEGGiheo:C694_07740.
hpy:HP1494.
PATRICi20594399. VBIHelPyl33062_1568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD08535.1 .
PIRi F64706.
RefSeqi NP_208285.1. NC_000915.1.
YP_006935420.1. NC_018939.1.

3D structure databases

ProteinModelPortali O26027.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O26027. 1 interaction.
STRINGi 85962.HP1494.

Proteomic databases

PRIDEi O26027.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD08535 ; AAD08535 ; HP_1494 .
GeneIDi 13870710.
899798.
KEGGi heo:C694_07740.
hpy:HP1494.
PATRICi 20594399. VBIHelPyl33062_1568.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci HPY:HP1494-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: ATCC 700392 / 26695.

Entry informationi

Entry nameiMURE_HELPY
AccessioniPrimary (citable) accession number: O26027
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 106 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. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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