A0QNG1 · PKNB_MYCS2
- ProteinSerine/threonine-protein kinase PknB
- GenepknB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids625 (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 (By similarity).
Probably phosphorylates RseA (PubMed:20025669).
Probably phosphorylates RseA (PubMed:20025669).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
By K-252a.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 17-25 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGFGGMSEV | ||||||
Binding site | 40 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 93-95 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EYV | ||||||
Active site | 138 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 140-143 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KPAN | ||||||
Binding site | 143 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 156 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 156 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | metal ion 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 PknB
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0QNG1
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 | 1-331 | Cytoplasmic | ||||
Sequence: MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGYSKQRSTSVARW | ||||||
Transmembrane | 332-352 | Helical | ||||
Sequence: LIAVAVLAVLTVVVTVAINMV | ||||||
Topological domain | 353-625 | Extracellular | ||||
Sequence: GGNPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
When depleted (with anti-sense RNA) no vancomycin-induced degradation of RseA is seen.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000422953 | 1-625 | Serine/threonine-protein kinase PknB | |||
Sequence: MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGYSKQRSTSVARWLIAVAVLAVLTVVVTVAINMVGGNPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA | ||||||
Modified residue | 169 | Phosphoserine; by autocatalysis | ||||
Sequence: S | ||||||
Modified residue | 171 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 173 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 294 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 295 | Phosphoserine; by autocatalysis | ||||
Sequence: S | ||||||
Modified residue | 309 | Phosphothreonine; by autocatalysis | ||||
Sequence: T |
Post-translational modification
Autophosphorylated. Dephosphorylated by PstP (By similarity).
Keywords
- PTM
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-274 | Protein kinase | ||||
Sequence: YELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLI | ||||||
Region | 302-321 | Disordered | ||||
Sequence: ADRAGAATQDMPVPRPAGYS | ||||||
Domain | 355-421 | PASTA 1 | ||||
Sequence: NPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVST | ||||||
Domain | 422-489 | PASTA 2 | ||||
Sequence: GPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGA | ||||||
Domain | 490-556 | PASTA 3 | ||||
Sequence: GPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSK | ||||||
Domain | 557-625 | PASTA 4 | ||||
Sequence: GNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA | ||||||
Region | 591-612 | Disordered | ||||
Sequence: DVRDSGQRTNAVVTQSPSAGTP | ||||||
Compositional bias | 597-612 | Polar residues | ||||
Sequence: QRTNAVVTQSPSAGTP |
Domain
The PASTA domains interact with peptidoglycans and are required for PknB localization.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length625
- Mass (Da)66,318
- Last updated2007-01-09 v1
- ChecksumE9B75950ADF718DA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 597-612 | Polar residues | ||||
Sequence: QRTNAVVTQSPSAGTP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK74027.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001663 EMBL· GenBank· DDBJ | AFP36514.1 EMBL· GenBank· DDBJ | Genomic DNA |