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Q8DJI4

- MURE_THEEB

UniProt

Q8DJI4 - MURE_THEEB

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Protein
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
Gene
murE, tlr1239
Organism
Thermosynechococcus elongatus (strain BP-1)
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 sitei32 – 321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei182 – 1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei188 – 1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei190 – 1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei385 – 3851Meso-diaminopimelate By similarity
Binding sitei460 – 4601Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding sitei464 – 4641Meso-diaminopimelate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi113 – 1197ATP Reviewed prediction

GO - Molecular functioni

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

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

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:tlr1239
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440: 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 – 497497UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseUniRule annotation
PRO_0000101959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221N6-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

Interactioni

Protein-protein interaction databases

STRINGi197221.tlr1239.

Structurei

3D structure databases

ProteinModelPortaliQ8DJI4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Regioni409 – 4124Meso-diaminopimelate binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi409 – 4124Meso-diaminopimelate recognition motifUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiVDYAHTG.
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.
InterProiIPR018109. Folylpolyglutamate_synth_CS.
IPR004101. 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.

Q8DJI4-1 [UniParc]FASTAAdd to Basket

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MNLRELLTAA AITPGFEHPA LNQEVKSLRM NSWECEPGSL FIGMPGTRVE    50
GGNFWPSALA AGAIAAVVSP QAKPREGEAC VIVVPDIERA CGRLAAAFYN 100
YPSQHLSLLG VTGTNGKTTT THLVEHLLNR VGYPTALLGT LYSRWPGHCE 150
VASHTTPFAV TLQEQLAAAV DAGCRFGVME VSSHALAQDR VWGCQFEVAA 200
FTNLTQDHLD YHRDLEDYFA AKAKLFTADY LKGRAILNGD DPFGQRLAQQ 250
LPRDRYWTYG LSKDADFRAE NLNYRSNGVT GAVHTPLGSG TLDSPLVGQF 300
NVANVLAAIA MGAAVGLPLE AMLNALRDFP GVPGRMEQVR LDPEQDITVV 350
VDYAHTPDSL ENLLRAARPF IPGKLICVFG CGGDRDRSKR PQMGAIAARL 400
ADQVVVTSDN PRTENPQRIL DDILAGIPPE TAMIVEGDRR QAILQAILTA 450
APGDGVIIAG KGHEDYQILG TEKVHFDDRE EARNALKERL KQPLQRG 497
Length:497
Mass (Da):53,933
Last modified:March 1, 2003 - v1
Checksum:i2F21F05584ECF07B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC08791.1.
RefSeqiNP_682029.1. NC_004113.1.
WP_011057081.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08791; BAC08791; BAC08791.
GeneIDi1011779.
KEGGitel:tlr1239.
PATRICi23927810. VBITheElo119873_1303.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC08791.1 .
RefSeqi NP_682029.1. NC_004113.1.
WP_011057081.1. NC_004113.1.

3D structure databases

ProteinModelPortali Q8DJI4.
ModBasei Search...

Protein-protein interaction databases

STRINGi 197221.tlr1239.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC08791 ; BAC08791 ; BAC08791 .
GeneIDi 1011779.
KEGGi tel:tlr1239.
PATRICi 23927810. VBITheElo119873_1303.

Phylogenomic databases

eggNOGi COG0769.
HOGENOMi HOG000268118.
KOi K01928.
OMAi VDYAHTG.
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 IPR018109. Folylpolyglutamate_synth_CS.
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: BP-1.

Entry informationi

Entry nameiMURE_THEEB
AccessioniPrimary (citable) accession number: Q8DJI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 82 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

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