A5TY85 · PKNA_MYCTA
- ProteinSerine/threonine-protein kinase PknA
- GenepknA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids431 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins such as FtsZ and MurD. Shows a strong preference for Thr versus Ser as the phosphoacceptor.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by magnesium or manganese. Inhibited by vanadate.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | regulation of primary metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase PknA
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionA5TY85
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-339 | Cytoplasmic | ||||
Sequence: MSPRVGVTLSGRYRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVAAVRAGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSRPATGGHRPPRRTFSSGQRA | ||||||
Transmembrane | 340-360 | Helical | ||||
Sequence: LLWAAGVLGALAIIIAVLLVI | ||||||
Topological domain | 361-431 | Extracellular | ||||
Sequence: KAPGDNSPQQAPTPTVTTTGNPPASNTGGTDASPRLNWTERGETRHSGLQSWVVPPTPHSRASLARYEIAQ |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 42 | Lack of autophosphorylation. | ||||
Sequence: K → M | ||||||
Mutagenesis | 172 | Strong decrease in autophosphorylation. | ||||
Sequence: T → A | ||||||
Mutagenesis | 174 | Decrease in autophosphorylation. | ||||
Sequence: T → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000419742 | 1-431 | Serine/threonine-protein kinase PknA | |||
Sequence: MSPRVGVTLSGRYRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVAAVRAGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSRPATGGHRPPRRTFSSGQRALLWAAGVLGALAIIIAVLLVIKAPGDNSPQQAPTPTVTTTGNPPASNTGGTDASPRLNWTERGETRHSGLQSWVVPPTPHSRASLARYEIAQ |
Post-translational modification
Autophosphorylated.
Keywords
- PTM
Interaction
Subunit
Interacts with FtsZ and MurD.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-272 | Protein kinase | ||||
Sequence: YRLQRLIATGGMGQVWEAVDNRLGRRVAVKVLKSEFSSDPEFIERFRAEARTTAMLNHPGIASVHDYGESQMNGEGRTAYLVMELVNGEPLNSVLKRTGRLSLRHALDMLEQTGRALQIAHAAGLVHRDVKPGNILITPTGQVKITDFGIAKAVDAAPVTQTGMVMGTAQYIAPEQALGHDASPASDVYSLGVVGYEAVSGKRPFAGDGALTVAMKHIKEPPPPLPPDLPPNVRELIEITLVKNPAMRYRSGGPFADAVA | ||||||
Region | 276-333 | Disordered | ||||
Sequence: AGRRPPRPSQTPPPGRAAPAAIPSGTTARVAANSAGRTAASRRSRPATGGHRPPRRTF | ||||||
Compositional bias | 302-316 | Polar residues | ||||
Sequence: TARVAANSAGRTAAS | ||||||
Compositional bias | 366-394 | Polar residues | ||||
Sequence: NSPQQAPTPTVTTTGNPPASNTGGTDASP | ||||||
Region | 366-418 | Disordered | ||||
Sequence: NSPQQAPTPTVTTTGNPPASNTGGTDASPRLNWTERGETRHSGLQSWVVPPTP | ||||||
Compositional bias | 403-417 | Polar residues | ||||
Sequence: ETRHSGLQSWVVPPT |
Domain
The kinase domain and the juxtamembrane region constitute the catalytic core of PknA. Interaction between core and C-terminal domains is crucial for activity.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)45,597
- Last updated2007-07-10 v1
- Checksum582D183747F3C111
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 302-316 | Polar residues | ||||
Sequence: TARVAANSAGRTAAS | ||||||
Compositional bias | 366-394 | Polar residues | ||||
Sequence: NSPQQAPTPTVTTTGNPPASNTGGTDASP | ||||||
Compositional bias | 403-417 | Polar residues | ||||
Sequence: ETRHSGLQSWVVPPT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000611 EMBL· GenBank· DDBJ | ABQ71735.1 EMBL· GenBank· DDBJ | Genomic DNA |