Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q97FC1 (MURE2_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase 2
EC=6.3.2.13
Alternative name(s):
Meso-A2pm-adding enzyme 2
Meso-diaminopimelate-adding enzyme 2
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase 2
UDP-MurNAc-tripeptide synthetase 2
UDP-N-acetylmuramyl-tripeptide synthetase 2
Gene names
Name:murE2
Ordered Locus Names:CA_C2819
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length483 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 HAMAP-Rule MF_00208.

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 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase 2 HAMAP-Rule MF_00208
PRO_0000101886

Regions

Nucleotide binding111 – 1177ATP Potential
Region156 – 1572UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region404 – 4074Meso-diaminopimelate binding By similarity
Motif404 – 4074Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3801Meso-diaminopimelate By similarity
Binding site4561Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4601Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2231N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97FC1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 5D0EAEC6F06B82E0

FASTA48353,845
        10         20         30         40         50         60 
MKLKQLLQNI DYDLIKGDIN INIEGISYNS KKVKQNYVFV SIKGARFDGH DFIKEAAQNG 

        70         80         90        100        110        120 
AAAVIIDEDF HDSIENTTLV KVKNSKVALA CLCNLFYEEP SRELNLVGVT GTNGKTTVIH 

       130        140        150        160        170        180 
YIRDMLEAFG NSTGTIGTLG YELKDKEINV EKINPTTPEA LELNQILRDF IDKGAKNAVM 

       190        200        210        220        230        240 
EVTSSALMKH RVDYCSFKVG VFTNLSQDHL DEHGTIENYK NEKIKLFKMC PVGVINLDDN 

       250        260        270        280        290        300 
IAGEIIEKGT CEFFTYGVLT NADLTASDMV YKPNSVSFNV HYKGISSKVK VNVPGEFTVY 

       310        320        330        340        350        360 
NVLAAIGSLL CLGIDFESIL KLVSSIKPVL GRLETINNPL NKNIIIDYAH TPDSLEKLLI 

       370        380        390        400        410        420 
MAREMTNGRI ITVFGCGGDR DKSKRGLMGM AVGILSDYCI ITSDNPRHEK PEDIIRDIER 

       430        440        450        460        470        480 
GMQTINSSYE KITDRRCAIK RGIEILKEED ILIIAGKGHE DYQIIGDNKV HFDDREVVNE 


LLG

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001437 Genomic DNA. Translation: AAK80763.1.
PIRH97246.
RefSeqNP_349423.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97FC1.
ModBaseSearch...

Protein-protein interaction databases

STRING272562.CA_C2819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK80763; AAK80763; CA_C2819.
GeneID1119002.
KEGGcac:CA_C2819.
PATRIC32040043. VBICloAce74127_3004.

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAFEDYLAC.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCACE272562:GJIH-2898-MONOMER.
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 nameMURE2_CLOAB
AccessionPrimary (citable) accession number: Q97FC1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2001
Last modified: May 1, 2013
This is version 87 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents