UniProt functional annotation for P39641



	UniProt functional annotation for P39641

UniProt code: P39641.

Organism: Bacillus subtilis (strain 168).

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.

Function: Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. In vivo catalyzes the ligation of L-alanine and L-anticapsin (epoxycyclohexanonyl-Ala) to produce the final bacilysin antibiotic (L- Ala-L-4S-cyclohexenonyl-Ala dipeptide). The substrate specificity is restricted to small amino acids such as L-Ala, for the N-terminal end of the dipeptide, whereas a wide range of hydrophobic amino acids such as L-Phe, L-Tyr and L-Met are recognized for the C-terminal end. {ECO:0000269|PubMed:15609023, ECO:0000269|PubMed:16030213, ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005, ECO:0000269|PubMed:24702628}.

Catalytic activity: Reaction=ATP + L-alanine + L-anticapsin = ADP + bacilysin + H(+) + phosphate; Xref=Rhea:RHEA:44332, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:84310, ChEBI:CHEBI:84311, ChEBI:CHEBI:456216; EC=6.3.2.49; Evidence={ECO:0000269|PubMed:16030213, ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005, ECO:0000269|PubMed:24702628};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628}; Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628};

Biophysicochemical properties: Kinetic parameters: KM=0.07 mM for ATP {ECO:0000269|PubMed:16030213}; KM=0.42 mM for L-alanine {ECO:0000269|PubMed:16030213}; KM=1.64 mM for L-alanine {ECO:0000269|PubMed:24702628}; KM=1.7 mM for L-alanine {ECO:0000269|PubMed:22407814}; KM=5.23 mM for L-phenylalanine {ECO:0000269|PubMed:24702628}; KM=20 mM for L-phenylalanine {ECO:0000269|PubMed:22407814}; KM=105.0 mM for L-glutamine {ECO:0000269|PubMed:16030213}; Vmax=0.764 umol/min/mg enzyme for Ala-Gln synthesis {ECO:0000269|PubMed:16030213}; Note=Kcat is 9.32 sec(-1) for ligase activity with alanine as substrate (PubMed:24702628). Kcat is 10.4 sec(-1) for ligase activity with phenylalanine as substrate (PubMed:24702628). Kcat is 630 min(- 1) for ligase activity with alanine and phenylalanine as substrate (PubMed:22407814). {ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628}; pH dependence: Optimum pH is 9.5. {ECO:0000269|PubMed:16030213}; Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16030213};

Pathway: Antibiotic biosynthesis; bacilysin biosynthesis. {ECO:0000305|PubMed:23317005}.

Subunit: Monomer or homodimer. {ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628}.

Induction: The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp) is essential for the transcription of the bacABCDE operon and GTP regulates the transcription of both this operon and ywfH via the CodY- mediated regulation system. {ECO:0000269|PubMed:12372825}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus subtilis (strain 168).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.



Function:		Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. In vivo catalyzes the ligation of L-alanine and L-anticapsin (epoxycyclohexanonyl-Ala) to produce the final bacilysin antibiotic (L- Ala-L-4S-cyclohexenonyl-Ala dipeptide). The substrate specificity is restricted to small amino acids such as L-Ala, for the N-terminal end of the dipeptide, whereas a wide range of hydrophobic amino acids such as L-Phe, L-Tyr and L-Met are recognized for the C-terminal end. {ECO:0000269\|PubMed:15609023, ECO:0000269\|PubMed:16030213, ECO:0000269\|PubMed:22407814, ECO:0000269\|PubMed:23317005, ECO:0000269\|PubMed:24702628}.


Catalytic activity:		Reaction=ATP + L-alanine + L-anticapsin = ADP + bacilysin + H(+) + phosphate; Xref=Rhea:RHEA:44332, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:84310, ChEBI:CHEBI:84311, ChEBI:CHEBI:456216; EC=6.3.2.49; Evidence={ECO:0000269\|PubMed:16030213, ECO:0000269\|PubMed:22407814, ECO:0000269\|PubMed:23317005, ECO:0000269\|PubMed:24702628};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:22407814, ECO:0000269\|PubMed:24702628}; Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000269\|PubMed:22407814, ECO:0000269\|PubMed:24702628};
Biophysicochemical properties:		Kinetic parameters: KM=0.07 mM for ATP {ECO:0000269\|PubMed:16030213}; KM=0.42 mM for L-alanine {ECO:0000269\|PubMed:16030213}; KM=1.64 mM for L-alanine {ECO:0000269\|PubMed:24702628}; KM=1.7 mM for L-alanine {ECO:0000269\|PubMed:22407814}; KM=5.23 mM for L-phenylalanine {ECO:0000269\|PubMed:24702628}; KM=20 mM for L-phenylalanine {ECO:0000269\|PubMed:22407814}; KM=105.0 mM for L-glutamine {ECO:0000269\|PubMed:16030213}; Vmax=0.764 umol/min/mg enzyme for Ala-Gln synthesis {ECO:0000269\|PubMed:16030213}; Note=Kcat is 9.32 sec(-1) for ligase activity with alanine as substrate (PubMed:24702628). Kcat is 10.4 sec(-1) for ligase activity with phenylalanine as substrate (PubMed:24702628). Kcat is 630 min(- 1) for ligase activity with alanine and phenylalanine as substrate (PubMed:22407814). {ECO:0000269\|PubMed:22407814, ECO:0000269\|PubMed:24702628}; pH dependence: Optimum pH is 9.5. {ECO:0000269\|PubMed:16030213}; Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269\|PubMed:16030213};
Pathway:		Antibiotic biosynthesis; bacilysin biosynthesis. {ECO:0000305\|PubMed:23317005}.
Subunit:		Monomer or homodimer. {ECO:0000269\|PubMed:22407814, ECO:0000269\|PubMed:24702628}.
Induction:		The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp) is essential for the transcription of the bacABCDE operon and GTP regulates the transcription of both this operon and ywfH via the CodY- mediated regulation system. {ECO:0000269\|PubMed:12372825}.