A0QNG1 · PKNB_MYCS2

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).

Catalytic activity

Activity regulation

By K-252a.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site17-25ATP (UniProtKB | ChEBI)
Binding site40ATP (UniProtKB | ChEBI)
Binding site93-95ATP (UniProtKB | ChEBI)
Active site138Proton acceptor
Binding site140-143ATP (UniProtKB | ChEBI)
Binding site143Mg2+ (UniProtKB | ChEBI)
Binding site156ATP (UniProtKB | ChEBI)
Binding site156Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processregulation of primary metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase PknB
  • EC number

Gene names

    • Name
      pknB
    • Ordered locus names
      MSMEG_0028, MSMEI_0031

Organism names

Accessions

  • Primary accession
    A0QNG1

Proteomes

Subcellular Location

Cell membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-331Cytoplasmic
Transmembrane332-352Helical
Topological domain353-625Extracellular

Keywords

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.

TypeIDPosition(s)Description
ChainPRO_00004229531-625Serine/threonine-protein kinase PknB
Modified residue169Phosphoserine; by autocatalysis
Modified residue171Phosphothreonine; by autocatalysis
Modified residue173Phosphothreonine; by autocatalysis
Modified residue294Phosphothreonine; by autocatalysis
Modified residue295Phosphoserine; by autocatalysis
Modified residue309Phosphothreonine; by autocatalysis

Post-translational modification

Autophosphorylated. Dephosphorylated by PstP (By similarity).

Keywords

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain11-274Protein kinase
Region302-321Disordered
Domain355-421PASTA 1
Domain422-489PASTA 2
Domain490-556PASTA 3
Domain557-625PASTA 4
Region591-612Disordered
Compositional bias597-612Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    625
  • Mass (Da)
    66,318
  • Last updated
    2007-01-09 v1
  • Checksum
    E9B75950ADF718DA
MTTPQHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPNGPLPYIVMEYVDGVTLRDIVHTDGPIAPRRAIEIIADACQALNFSHQHGIIHRDVKPANIMISKNNAVKVMDFGIARALADTGNSVTQTAAVIGTAQYLSPEQARGETVDARSDVYSLGCVLYEILTGEPPFIGDSPVAVAYQHVREDPVPPSRRHADVTPELDAVVLKALAKNPDNRYQTAAEMRADLIRVHEGQAPDAPKVLTDAERTSMLAAPPADRAGAATQDMPVPRPAGYSKQRSTSVARWLIAVAVLAVLTVVVTVAINMVGGNPRNVQVPDVAEQSADDAQAALQNRGFKTVIDRQPDNEVPPGLVIGTDPEAGSELGAGEQVTINVSTGPEQALVPDVAGLTPTQARQKLKDAGFEKFRESPSPSTPEQKGRVLATNPQANQTAAIINEITIVVGAGPEDAPVLSCAGQNAESCKAILAAGGFTNTVVVEVDNPAAAGQVVGTEPADGQSVPKDTVIQIRVSKGNQFVMPDLVGQFWSDAYPRLTALGWTGVLDKGPDVRDSGQRTNAVVTQSPSAGTPVNKDAKITLSFAA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias597-612Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000480
EMBL· GenBank· DDBJ
ABK74027.1
EMBL· GenBank· DDBJ
Genomic DNA
CP001663
EMBL· GenBank· DDBJ
AFP36514.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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