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Q8ZRU7 (MURE_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:murE
Ordered Locus Names:STM0123
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00208

Catalytic activity

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. HAMAP-Rule MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00208

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP-Rule MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101937

Regions

Nucleotide binding116 – 1227ATP Potential
Region44 – 463UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region158 – 1592UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region414 – 4174Meso-diaminopimelate binding By similarity
Motif414 – 4174Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site271UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1571UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1931UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3901Meso-diaminopimelate By similarity
Binding site4651Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4691Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2251N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZRU7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 3C5FDBA7BEFDB393

FASTA49553,287
        10         20         30         40         50         60 
MADRNLRDLL APWVAGLPAR ELREMTLDSR VAAAGDLFVA VVGHQADGRR YIPQAIAQGV 

        70         80         90        100        110        120 
AAIIAEAKDE ASDGEIREMH GVPVVYLSQL NERLSALAGR FYHEPSENMR LVAVTGTNGK 

       130        140        150        160        170        180 
TTTTQLLAQW SQLLGETSAV MGTVGNGLLG KVIPTENTTG SAVDVQHVLA SLVAQGATFG 

       190        200        210        220        230        240 
AMEVSSHGLV QHRVAALKFA ASVFTNLSRD HLDYHGDMAH YEAAKWMLYS THHHGQAIVN 

       250        260        270        280        290        300 
ADDEVGRRWL ASLPDAVAVS MEGHINPNCH GRWLKAEAVE YHDRGATIRF ASSWGEGEIE 

       310        320        330        340        350        360 
SRLMGAFNVS NLLLALATLL ALGYPLTDLL KTAARLQPVC GRMEVFTAPG KPTVVVDYAH 

       370        380        390        400        410        420 
TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA IAEEFADIVV VTDDNPRTEE 

       430        440        450        460        470        480 
PRAIINDILA GMLDAGQVRV MEGRAEAVTN AIMQAKDNDV VLIAGKGHED YQIVGTQRLD 

       490 
YSDRVTAARL LGVIA

« Hide

References

[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006468 Genomic DNA. Translation: AAL19087.1.
RefSeqNP_459128.1. NC_003197.1.

3D structure databases

ProteinModelPortalQ8ZRU7.
SMRQ8ZRU7. Positions 3-495.
ModBaseSearch...

Protein-protein interaction databases

STRING99287.STM0123.

Proteomic databases

PaxDbQ8ZRU7.
PRIDEQ8ZRU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19087; AAL19087; STM0123.
GeneID1251641.
KEGGstm:STM0123.
PATRIC32378519. VBISalEnt20916_0129.

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_SALTY
AccessionPrimary (citable) accession number: Q8ZRU7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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