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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_RICFE              Reviewed;         530 AA.
Q4UMI9;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
28-FEB-2018, entry version 100.
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=RF_0368;
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
NCBI_TaxID=315456;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-1525 / URRWXCal2;
PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
Parinello H., Claverie J.-M., Raoult D.;
"The genome sequence of Rickettsia felis identifies the first putative
conjugative plasmid in an obligate intracellular parasite.";
PLoS Biol. 3:1-12(2005).
-!- 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; CP000053; AAY61219.1; -; Genomic_DNA.
RefSeq; WP_011270707.1; NC_007109.1.
ProteinModelPortal; Q4UMI9; -.
STRING; 315456.RF_0368; -.
EnsemblBacteria; AAY61219; AAY61219; RF_0368.
KEGG; rfe:RF_0368; -.
eggNOG; ENOG4107EEN; Bacteria.
eggNOG; COG0769; LUCA.
HOGENOM; HOG000268118; -.
KO; K01928; -.
OMA; CFMEVSS; -.
OrthoDB; POG091H0082; -.
UniPathway; UPA00219; -.
Proteomes; UP000008548; 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; -; 2.
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; IPR005728; Rickett_RPE.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 2.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 2.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR01085; murE; 1.
TIGRFAMs; TIGR01045; RPE1; 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.
CHAIN 1 530 UDP-N-acetylmuramoyl-L-alanyl-D-
glutamate--2,6-diaminopimelate ligase.
/FTId=PRO_0000278039.
DOMAIN 221 269 RPE1 insert.
NP_BIND 99 105 ATP. {ECO:0000255|HAMAP-Rule:MF_00208}.
REGION 145 146 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000255|HAMAP-Rule:MF_00208}.
REGION 446 449 Meso-diaminopimelate binding.
{ECO:0000255|HAMAP-Rule:MF_00208}.
MOTIF 446 449 Meso-diaminopimelate recognition motif.
BINDING 21 21 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 172 172 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 180 180 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 422 422 Meso-diaminopimelate. {ECO:0000255|HAMAP-
Rule:MF_00208}.
BINDING 496 496 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000255|HAMAP-
Rule:MF_00208}.
BINDING 500 500 Meso-diaminopimelate. {ECO:0000255|HAMAP-
Rule:MF_00208}.
MOD_RES 212 212 N6-carboxylysine. {ECO:0000255|HAMAP-
Rule:MF_00208}.
SEQUENCE 530 AA; 59450 MW; DB0F36484D2E8508 CRC64;
MPYNLKQLFQ KHNVKGLSIN SKTVKENDIF FAIKGQNVDG NDFINEVLNQ AVALVITDNK
KNTIIDDKVI YVEDVQVALY EAIEIFYPKK PKNLIAVTGT NGKSSVVSYI AQTYSLLGKK
AASIGTIGVE IFGCDNLIND VPELTTLDYL SFRKIAHNLA ENNIEYLAFE ASSHGLNQAR
LGEIKVNTAC FTSFSQDHLD YHHTKENYLL AKLKLFTRHL FKPAYREEFK GDTEHSTTAY
ILVREDASTG STSKLLLEAK FGKMSTEYLL QGGLAILNSD IAEIEFVKDY LRNHNIKFIT
VGKKGDVQIT KINGSLKAQN INFIFNNREC SFNTSIIGSF QASNLLIAAL SIHYIGFDFN
KIIEILTQVK PVKGRMERIG NTNIFVDYSH TPDALEKALT ELKNVKLRDS RLNVVFGCGG
NRDKTKRSLM GQIAARLADN VIITDDNPRH EDPKLIRAEI ISGIEKADYT EIANREEAIK
YGINNLKQDD ILLIAGKGHE NYQIIGDKKL PFDDAEIVRK LMSLRGKAKP


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