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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (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)

 MURE_CHLPN              Reviewed;         483 AA.
Q9Z8C5; Q9JQA1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 134.
RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208};
EC=6.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=Meso-A2pm-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
Name=murE {ECO:0000255|HAMAP-Rule:MF_00208};
OrderedLocusNames=CPn_0418, CP_0336, CpB0434;
Chlamydia pneumoniae (Chlamydophila pneumoniae).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=83558;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CWL029;
PubMed=10192388; DOI=10.1038/7716;
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
"Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
Nat. Genet. 21:385-389(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AR39;
PubMed=10684935; DOI=10.1093/nar/28.6.1397;
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J138;
PubMed=10871362; DOI=10.1093/nar/28.12.2311;
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
"Comparison of whole genome sequences of Chlamydia pneumoniae J138
from Japan and CWL029 from USA.";
Nucleic Acids Res. 28:2311-2314(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW-183;
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
"The genome sequence of Chlamydia pneumoniae TW183 and comparison with
other Chlamydia strains based on whole genome sequence analysis.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
-!- 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.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate +
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-
diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00208}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00208};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
-!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
consequently, for the gamma-phosphate positioning of ATP.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-----------------------------------------------------------------------
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EMBL; AE001363; AAD18562.1; -; Genomic_DNA.
EMBL; AE002161; AAF38190.1; -; Genomic_DNA.
EMBL; BA000008; BAA98626.1; -; Genomic_DNA.
EMBL; AE009440; AAP98365.1; -; Genomic_DNA.
PIR; D72080; D72080.
PIR; H86542; H86542.
RefSeq; NP_224618.1; NC_000922.1.
RefSeq; WP_010883061.1; NZ_LN847257.1.
ProteinModelPortal; Q9Z8C5; -.
SMR; Q9Z8C5; -.
STRING; 182082.CpB0434; -.
PRIDE; Q9Z8C5; -.
EnsemblBacteria; AAD18562; AAD18562; CPn_0418.
EnsemblBacteria; AAF38190; AAF38190; CP_0336.
EnsemblBacteria; AAP98365; AAP98365; CpB0434.
EnsemblBacteria; BAA98626; BAA98626; BAA98626.
GeneID; 894904; -.
KEGG; cpa:CP_0336; -.
KEGG; cpj:murE; -.
KEGG; cpn:CPn0418; -.
KEGG; cpt:CpB0434; -.
PATRIC; fig|115713.3.peg.462; -.
eggNOG; ENOG4107EEN; Bacteria.
eggNOG; COG0769; LUCA.
HOGENOM; HOG000268118; -.
KO; K01928; -.
OMA; CFMEVSS; -.
OrthoDB; POG091H0082; -.
UniPathway; UPA00219; -.
Proteomes; UP000000583; Chromosome.
Proteomes; UP000000801; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00208; MurE; 1.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR01085; murE; 1.
3: Inferred from homology;
ATP-binding; Cell cycle; Cell division; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Ligase; Magnesium; Nucleotide-binding; Peptidoglycan synthesis;
Reference proteome.
CHAIN 1 483 UDP-N-acetylmuramoyl-L-alanyl-D-
glutamate--2,6-diaminopimelate ligase.
/FTId=PRO_0000101881.
NP_BIND 109 115 ATP. {ECO:0000255|HAMAP-Rule:MF_00208}.
REGION 151 152 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000255|HAMAP-Rule:MF_00208}.
REGION 403 406 Meso-diaminopimelate binding.
{ECO:0000255|HAMAP-Rule:MF_00208}.
MOTIF 403 406 Meso-diaminopimelate recognition motif.
BINDING 30 30 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 178 178 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 186 186 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 380 380 Meso-diaminopimelate. {ECO:0000255|HAMAP-
Rule:MF_00208}.
BINDING 453 453 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000255|HAMAP-
Rule:MF_00208}.
BINDING 457 457 Meso-diaminopimelate. {ECO:0000255|HAMAP-
Rule:MF_00208}.
MOD_RES 218 218 N6-carboxylysine. {ECO:0000255|HAMAP-
Rule:MF_00208}.
SEQUENCE 483 AA; 52720 MW; 3A0FEEA93EDD76ED CRC64;
MDLKELLHGV QAKIYGKVRP LEVRNLTRDS RCVSVGDIFI AHKGQRYDGN DFAVDALANG
AIAIASSLYN PFLSVVQIIT PNLEELEAEL SAKYYEYPSS KLHTIGVTGT NGKTTVTCLI
KALLDSYQKP SGLLGTIEHI LGEGVIKDGF TTPTPALLQK YLATMVRQNR DAVVMEVSSI
GLASGRVAYT NFDTAVLTNI TLDHLDFHGT FETYVAAKAK LFSLVPPSGM VVINTDSPYA
SQCIESAKAP VITYGIESAA DYRATDIQLS SSGTKYTLVY GDQKIACSSS FIGKYNVYNL
LAAISTVHAS LRCDLEDLLE KIGLCQPPPG RLDPVLMGPC PVYIDYAHTP DALDNVLTGL
HELLPEGGRL IVVFGCGGDR DRSKRKLMAQ VVERYGFAVV TSDNPRSEPP EDIVNEICDG
FYSKNYFIEI DRKQAITYAL SIASDRDIVL IAGKGHEAYQ IFKHQTVAFD DKQTVCEVLA
SYV


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