P9WI83

EV
Gene name
pknA (Rv0015c, MTCY10H4.15c)
Protein name
Serine/threonine-protein kinase PknA
Names
EC 2.7.11.1
Species
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
KEGG Pathway
mtu:Rv0015c
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class
MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED (PTHR43289)

Descriptions

PknA is a serine/threonine-protein kinase involved in regulating cell division and cell wall synthesis in Mycobacterium tuberculosis. It is essential for the pathogen's survival. Autoinhibition in PknA is maintained by a Src-like conformation where the N-terminal lobe and C-terminal lobe are held in an inactive state by the positioning of the activation loop, preventing substrate binding and catalysis. This autoinhibition is relieved by phosphorylation of the activation loop, which triggers a conformational change to an active state.

Autoinhibitory domains (AIDs)

Accessory elements

158-166 (Activation loop from InterPro)

Target domain

12-274 (Kinase domain)

Relief mechanism

PTM

Assay

Structural analysis, Mutagenesis experiment

175-182 (Activation loop from InterPro)

Target domain

12-274 (Kinase domain)

Relief mechanism

PTM

Assay

Structural analysis, Mutagenesis experiment

References

Autoinhibited structure

Activated structure

4 structures for P9WI83

Entry ID Method Resolution Chain Position Source
4OW8 X-ray 203 A A 1-283 PDB
4X3F X-ray 290 A A/B/C 1-336 PDB
6B2Q X-ray 288 A A/B/C/D 1-296 PDB
AF-P9WI83-F1 Predicted AlphaFoldDB

No variants for P9WI83

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WI83

No associated diseases with P9WI83

2 regional properties for P9WI83

Type Name Position InterPro Accession
domain Protein kinase domain 13 - 272 IPR000719
active_site Serine/threonine-protein kinase, active site 137 - 149 IPR008271

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cell membrane ; Single-pass membrane protein
  • The majority of the cells displays PknA expression at the membrane perimeter along the length of the cell, whereas a minor population shows PknA to localize at either or both poles (uni- and bipolar; 16 and 14%, respectively) and occasionally to both the poles and the midcell (12%)
PANTHER Family PTHR43289 MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED
PANTHER Subfamily PTHR43289:SF37 SERINE_THREONINE-PROTEIN KINASE A
PANTHER Protein Class non-receptor serine/threonine protein kinase
protein modifying enzyme
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction
protein serine kinase activity Catalysis of the reactions
protein serine/threonine kinase activity Catalysis of the reactions

9 GO annotations of biological process

Name Definition
negative regulation of catalytic activity Any process that stops or reduces the activity of an enzyme.
negative regulation of fatty acid biosynthetic process Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids.
negative regulation of lipid biosynthetic process Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of lipids.
peptidyl-threonine autophosphorylation The phosphorylation by a protein of one or more of its own threonine amino acid residues, or a threonine residue on an identical protein.
positive regulation of catalytic activity Any process that activates or increases the activity of an enzyme.
positive regulation of DNA binding Any process that increases the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
protein phosphorylation The process of introducing a phosphate group on to a protein.
regulation of cell shape Any process that modulates the surface configuration of a cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSPRVGVTLS GRYRLQRLIA TGGMGQVWEA VDNRLGRRVA VKVLKSEFSS DPEFIERFRA
70 80 90 100 110 120
EARTTAMLNH PGIASVHDYG ESQMNGEGRT AYLVMELVNG EPLNSVLKRT GRLSLRHALD
130 140 150 160 170 180
MLEQTGRALQ IAHAAGLVHR DVKPGNILIT PTGQVKITDF GIAKAVDAAP VTQTGMVMGT
190 200 210 220 230 240
AQYIAPEQAL GHDASPASDV YSLGVVGYEA VSGKRPFAGD GALTVAMKHI KEPPPPLPPD
250 260 270 280 290 300
LPPNVRELIE ITLVKNPAMR YRSGGPFADA VAAVRAGRRP PRPSQTPPPG RAAPAAIPSG
310 320 330 340 350 360
TTARVAANSA GRTAASRRSR PATGGHRPPR RTFSSGQRAL LWAAGVLGAL AIIIAVLLVI
370 380 390 400 410 420
KAPGDNSPQQ APTPTVTTTG NPPASNTGGT DASPRLNWTE RGETRHSGLQ SWVVPPTPHS
430
RASLARYEIA Q