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Q9Z8C5

- MURE_CHLPN

UniProt

Q9Z8C5 - MURE_CHLPN

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Protein
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
Gene
murE, CPn_0418, CP_0336, CpB0434
Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
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 sitei178 – 1781UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei186 – 1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding sitei380 – 3801Meso-diaminopimelate By similarity
Binding sitei453 – 4531Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding sitei457 – 4571Meso-diaminopimelate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1157ATP 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

GO - Biological processi

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

BioCyciCPNE115711:GI7B-349-MONOMER.
CPNE115713:GHEY-434-MONOMER.
CPNE138677:GH8N-429-MONOMER.
CPNE182082:GH4N-446-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:CPn_0418, CP_0336, CpB0434
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: 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 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseUniRule annotation
PRO_0000101881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181N6-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

STRINGi115713.CPn0418.

Structurei

3D structure databases

ProteinModelPortaliQ9Z8C5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1522UDP-MurNAc-L-Ala-D-Glu binding By similarity
Regioni403 – 4064Meso-diaminopimelate binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi403 – 4064Meso-diaminopimelate recognition motifUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0769.
HOGENOMiHOG000268118.
KOiK01928.
OMAiAVMTNLS.
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.

Q9Z8C5-1 [UniParc]FASTAAdd to Basket

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MDLKELLHGV QAKIYGKVRP LEVRNLTRDS RCVSVGDIFI AHKGQRYDGN    50
DFAVDALANG AIAIASSLYN PFLSVVQIIT PNLEELEAEL SAKYYEYPSS 100
KLHTIGVTGT NGKTTVTCLI KALLDSYQKP SGLLGTIEHI LGEGVIKDGF 150
TTPTPALLQK YLATMVRQNR DAVVMEVSSI GLASGRVAYT NFDTAVLTNI 200
TLDHLDFHGT FETYVAAKAK LFSLVPPSGM VVINTDSPYA SQCIESAKAP 250
VITYGIESAA DYRATDIQLS SSGTKYTLVY GDQKIACSSS FIGKYNVYNL 300
LAAISTVHAS LRCDLEDLLE KIGLCQPPPG RLDPVLMGPC PVYIDYAHTP 350
DALDNVLTGL HELLPEGGRL IVVFGCGGDR DRSKRKLMAQ VVERYGFAVV 400
TSDNPRSEPP EDIVNEICDG FYSKNYFIEI DRKQAITYAL SIASDRDIVL 450
IAGKGHEAYQ IFKHQTVAFD DKQTVCEVLA SYV 483
Length:483
Mass (Da):52,720
Last modified:May 1, 1999 - v1
Checksum:i3A0FEEA93EDD76ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001363 Genomic DNA. Translation: AAD18562.1.
AE002161 Genomic DNA. Translation: AAF38190.1.
BA000008 Genomic DNA. Translation: BAA98626.1.
AE009440 Genomic DNA. Translation: AAP98365.1.
PIRiD72080.
H86542.
RefSeqiNP_224618.1. NC_000922.1.
NP_300475.1. NC_002491.1.
NP_444885.1. NC_002179.2.
NP_876708.1. NC_005043.1.

Genome annotation databases

EnsemblBacteriaiAAD18562; AAD18562; CPn_0418.
AAF38190; AAF38190; CP_0336.
AAP98365; AAP98365; CpB0434.
BAA98626; BAA98626; BAA98626.
GeneIDi1467115.
894904.
919161.
962867.
KEGGicpa:CP0336.
cpj:CPj0418.
cpn:CPn0418.
cpt:CpB0434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001363 Genomic DNA. Translation: AAD18562.1 .
AE002161 Genomic DNA. Translation: AAF38190.1 .
BA000008 Genomic DNA. Translation: BAA98626.1 .
AE009440 Genomic DNA. Translation: AAP98365.1 .
PIRi D72080.
H86542.
RefSeqi NP_224618.1. NC_000922.1.
NP_300475.1. NC_002491.1.
NP_444885.1. NC_002179.2.
NP_876708.1. NC_005043.1.

3D structure databases

ProteinModelPortali Q9Z8C5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 115713.CPn0418.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD18562 ; AAD18562 ; CPn_0418 .
AAF38190 ; AAF38190 ; CP_0336 .
AAP98365 ; AAP98365 ; CpB0434 .
BAA98626 ; BAA98626 ; BAA98626 .
GeneIDi 1467115.
894904.
919161.
962867.
KEGGi cpa:CP0336.
cpj:CPj0418.
cpn:CPn0418.
cpt:CpB0434.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci CPNE115711:GI7B-349-MONOMER.
CPNE115713:GHEY-434-MONOMER.
CPNE138677:GH8N-429-MONOMER.
CPNE182082:GH4N-446-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: CWL029.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AR39.
  3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
    Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
    Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J138.
  4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
    Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TW-183.

Entry informationi

Entry nameiMURE_CHLPN
AccessioniPrimary (citable) accession number: Q9Z8C5
Secondary accession number(s): Q9JQA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 108 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

Documents

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

External Data

Dasty 3

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