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Q83F28

- MURE_COXBU

UniProt

Q83F28 - MURE_COXBU

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Protein
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
Gene
murE, CBU_0123
Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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 sitei30 – 301UDP-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 sitei388 – 3881Meso-diaminopimelate By similarity
Binding sitei463 – 4631Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding sitei467 – 4671Meso-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. acid-amino acid ligase activity Source: TIGR

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. peptidoglycan biosynthetic process Source: TIGR
  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

BioCyciCBUR227377:GJ7S-128-MONOMER.
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:CBU_0123
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000002671: 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 – 489489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseUniRule annotation
PRO_0000101891Add
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

STRINGi227377.CBU_0123.

Structurei

3D structure databases

ProteinModelPortaliQ83F28.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Regioni412 – 4154Meso-diaminopimelate binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi412 – 4154Meso-diaminopimelate recognition motifUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiKIAVDYA.
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.
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.

Q83F28-1 [UniParc]FASTAAdd to Basket

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MNGKYLSQLL DAKNKALTAD VLIKALQTDS RKIQPGDLFI AYPGLQVDGR    50
DYIKEALDKK AAAVFYEANQ YNPSIQTKVP LIPFENLQHR IGEIAARFYD 100
DPSCEMEIIG ITGTNGKTSC AQFIAQALQS QGIRCGVIGT LGYGFLGSLH 150
KTSHTTPEPI QLQQAFAEMR KQGAKAIAME VSSHALHQRR VEGVQFDIAV 200
FTQLSRDHLD YHGDMENYAR AKELLFQQPG LHTGVVNCDD ALGKRIIAHY 250
RHQLTLVGYS ANGVKDDRVS SVIASAIQPL AQGFSVEVQT PWGEGTFTTP 300
LFGRFNISNL LAVLSVLCLC EIPFDKALLE LSQLRNVPGR MQVVDSQRQP 350
QIIVDYAHTP DALEKALTAL REHCQGRLIC VFGCGGDRDR GKRPQMAAVA 400
EQHADQIILT NDNPRTESPL TIIQDIQAGF KNKNAVLVKL DRAEAIRYAV 450
QMAAVNDIVL IAGKGHETTQ TIADQVLPFN DVEEAKKAL 489
Length:489
Mass (Da):53,828
Last modified:June 1, 2003 - v1
Checksum:i6AC4716157215B22
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016828 Genomic DNA. Translation: AAO89687.1.
RefSeqiNP_819173.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO89687; AAO89687; CBU_0123.
GeneIDi1207994.
KEGGicbu:CBU_0123.
PATRICi17928931. VBICoxBur82552_0126.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016828 Genomic DNA. Translation: AAO89687.1 .
RefSeqi NP_819173.1. NC_002971.3.

3D structure databases

ProteinModelPortali Q83F28.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227377.CBU_0123.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO89687 ; AAO89687 ; CBU_0123 .
GeneIDi 1207994.
KEGGi cbu:CBU_0123.
PATRICi 17928931. VBICoxBur82552_0126.

Phylogenomic databases

eggNOGi COG0769.
HOGENOMi HOG000268118.
KOi K01928.
OMAi KIAVDYA.
OrthoDBi EOG6PKFCR.

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci CBUR227377:GJ7S-128-MONOMER.

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 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: RSA 493 / Nine Mile phase I.

Entry informationi

Entry nameiMURE_COXBU
AccessioniPrimary (citable) accession number: Q83F28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 78 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. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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