UniProt functional annotation for P22188



	UniProt functional annotation for P22188

UniProt code: P22188.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine. {ECO:0000269|PubMed:11124264, ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:3905407}.

Catalytic activity: Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D- muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N- acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000269|PubMed:11124264, ECO:0000269|PubMed:2269304};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00208};

Activity regulation: Activated by potassium phosphate. {ECO:0000269|PubMed:2269304}.

Biophysicochemical properties: Kinetic parameters: KM=76 uM for UDP-N-acetylmuramoyl-L-Ala-D-Glu {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; KM=36 uM for meso-diaminopimelate {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; KM=1500 uM for meso-lanthionine {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; KM=3900 uM for L-allo-cystathionine {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; KM=10000 uM for D-allo-cystathionine {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; KM=620 uM for ATP {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; Vmax=32 nmol/min/mg enzyme with meso-diaminopimelate as substrate {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; Vmax=23 nmol/min/mg enzyme with meso-lanthionine as substrate {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; Vmax=19 nmol/min/mg enzyme with L-allo-cystathionine as substrate {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; Vmax=23 nmol/min/mg enzyme with L-allo-cystathionine as substrate {ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:8021219}; pH dependence: Optimum pH is about 8. {ECO:0000269|PubMed:2269304};

Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.

Subcellular location: Cytoplasm {ECO:0000305}.

Ptm: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP. {ECO:0000269|PubMed:11124264}.

Similarity: Belongs to the MurCDEF family. MurE subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine. {ECO:0000269\|PubMed:11124264, ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:3905407}.


Catalytic activity:		Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D- muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N- acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13; Evidence={ECO:0000269\|PubMed:11124264, ECO:0000269\|PubMed:2269304};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255\|HAMAP-Rule:MF_00208};
Activity regulation:		Activated by potassium phosphate. {ECO:0000269\|PubMed:2269304}.
Biophysicochemical properties:		Kinetic parameters: KM=76 uM for UDP-N-acetylmuramoyl-L-Ala-D-Glu {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; KM=36 uM for meso-diaminopimelate {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; KM=1500 uM for meso-lanthionine {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; KM=3900 uM for L-allo-cystathionine {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; KM=10000 uM for D-allo-cystathionine {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; KM=620 uM for ATP {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; Vmax=32 nmol/min/mg enzyme with meso-diaminopimelate as substrate {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; Vmax=23 nmol/min/mg enzyme with meso-lanthionine as substrate {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; Vmax=19 nmol/min/mg enzyme with L-allo-cystathionine as substrate {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; Vmax=23 nmol/min/mg enzyme with L-allo-cystathionine as substrate {ECO:0000269\|PubMed:2269304, ECO:0000269\|PubMed:8021219}; pH dependence: Optimum pH is about 8. {ECO:0000269\|PubMed:2269304};
Pathway:		Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location:		Cytoplasm {ECO:0000305}.
Ptm:		Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP. {ECO:0000269\|PubMed:11124264}.
Similarity:		Belongs to the MurCDEF family. MurE subfamily. {ECO:0000305}.