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Protein

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

Gene

murE

Organism
Rickettsia rickettsii
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathway:ipeptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei171 – 1711UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei177 – 1771UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei179 – 1791UDP-MurNAc-L-Ala-D-GluUniRule annotation
Binding sitei372 – 3721Meso-diaminopimelateUniRule annotation
Binding sitei446 – 4461Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
Binding sitei450 – 4501Meso-diaminopimelateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi98 – 1047ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

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, Magnesium, 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
OrganismiRickettsia rickettsii
Taxonomic identifieri783 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111N6-carboxylysineUniRule annotation

Post-translational modificationi

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

Structurei

3D structure databases

ProteinModelPortaliQ9AKI7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 1452UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
Regioni396 – 3994Meso-diaminopimelate bindingUniRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi396 – 3994Meso-diaminopimelate recognition motif

Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

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.

Q9AKI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHNLKQLFQ QHNVKGLSIN SKTVKDKDIF FAIKGRNTDG NDFIKDALSK
60 70 80 90 100
GAVLVITDNK KNIVIDKVIY VKDVQAALYE AIEIFYPKKP KDLIAVTGTN
110 120 130 140 150
GKSSVVSYIA QTYSLLGKKA ASIGTIGVEI FGCVNLINDV PELTTLDYLS
160 170 180 190 200
FRKIAHNLAE NGIEYLVFEA SSHGLDQARL REIKVNIACF TSFSQDHLDY
210 220 230 240 250
HHTKENYLLA KLKLFINHLL PNGIAILNSD IEEIEFVKDY LHNHNVKFIT
260 270 280 290 300
VGTKGDLEIT RLNCSLKGQN INFTFNNREY NFNTPIIGSF QASNLLIAVL
310 320 330 340 350
SIHYIGFAFD DVIDSLVEVK AVKGRMERID NTNIFVDYAH TPDALEKALT
360 370 380 390 400
ELKNIKLRDS KLSVVFGCGG NRDKAKRSLM GQIAAKRADT IIITDDNPRH
410 420 430 440 450
EDPKLIRAEI ISGIEKADYT EIANREEAIK YGINNLKQDD ILLVAGKGHE
460 470
NYQIIGDKKL PFDDAEVVRK CIKVCHPVA
Length:479
Mass (Da):53,640
Last modified:June 1, 2001 - v1
Checksum:iBE5379B53EC28326
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293314 Genomic DNA. Translation: CAC33671.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ293314 Genomic DNA. Translation: CAC33671.1.

3D structure databases

ProteinModelPortaliQ9AKI7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00219.

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.
ProtoNetiSearch...

Publicationsi

  1. "Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes."
    Andersson J.O., Andersson S.G.E.
    Mol. Biol. Evol. 18:829-839(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 84-21C.

Entry informationi

Entry nameiMURE_RICRI
AccessioniPrimary (citable) accession number: Q9AKI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.