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Q87SG9 (MURE_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. 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:VP0455
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length493 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 – 493493UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101968

Regions

Nucleotide binding117 – 1237ATP Potential
Region159 – 1602UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region412 – 4154Meso-diaminopimelate binding By similarity
Motif412 – 4154Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1581UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1921UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1941UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3881Meso-diaminopimelate By similarity
Binding site4631Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4671Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2261N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87SG9 [UniParc].

Last modified May 30, 2003. Version 1.
Checksum: 4FB0765E7FF37869

FASTA49352,986
        10         20         30         40         50         60 
MTKAISMDAL LSPWVDCPSL ASVLVSELEL DSRKVQPGTT FVALVGHVVD GRKFIASAIE 

        70         80         90        100        110        120 
KGANAVIAQA CDVKAHGTID IIDDIPVVYL DALDKCLSEI AGQLYTYPDM KLIGVTGTNG 

       130        140        150        160        170        180 
KTTITQLIAQ WIGLVGSKAA VMGTTGNGFL DDLKEAANTT GNAVEIQHTL ASLAEQQAQY 

       190        200        210        220        230        240 
TALEVSSHGL IQGRVKSLSF AAGVFTNLSR DHLDYHGTME EYANAKLTLF TQHQCAQAII 

       250        260        270        280        290        300 
NVDDEVGAAW AKQLTNAIAV SLAPTTEFEH ALWASQVAYA ESGITIRFDG QFGEGTLHAP 

       310        320        330        340        350        360 
LIGEFNAANL MLAFATLLSL GFDKSDLLAT AAQLQPVLGR MELFQAEHRA KVVVDYAHTP 

       370        380        390        400        410        420 
DALEKALQAL RVHCDGQLWA IFGCGGDRDA GKRPMMAEIA ERLGDKVVLT DDNPRSEDPV 

       430        440        450        460        470        480 
LIVKDMLAGL SKPAEAIVQH DRFKALFYAL ENAAPQDIIL LAGKGHEDYQ IRNGETIHYS 

       490 
DRESAMQLLG LSS

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000031 Genomic DNA. Translation: BAC58718.1.
RefSeqNP_796834.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87SG9.
SMRQ87SG9. Positions 8-490.
ModBaseSearch...

Protein-protein interaction databases

STRING223926.VP0455.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC58718; BAC58718; BAC58718.
GeneID1187923.
KEGGvpa:VP0455.
PATRIC20139118. VBIVibPar50997_0433.

Organism-specific databases

CMRSearch...

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_VIBPA
AccessionPrimary (citable) accession number: Q87SG9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 30, 2003
Last modified: May 1, 2013
This is version 74 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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