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MYCTU:PKNH

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) pknH
Protein Name(s) Serine/threonine-protein kinase PknH
External Links
UniProt P9WI71
EMBL AL123456
PIR B70754
RefSeq NP_215782.1
WP_010886110.1
PDB 4ESQ
PDBsum 4ESQ
ProteinModelPortal P9WI71
SMR P9WI71
GeneID 887023
KEGG mtu:Rv1266c
TubercuList Rv1266c
KO K08884
OMA APERFAN
Proteomes UP000001584
GO GO:0005618
GO:0005887
GO:0005524
GO:0004672
GO:0004674
GO:0043086
GO:0045926
GO:0043085
GO:0043388
GO:0045893
GO:0046777
GO:0046890
GO:0052572
InterPro IPR011009
IPR026954
IPR000719
IPR017441
IPR008271
Pfam PF00069
PF14032
SUPFAM SSF56112
PROSITE PS00107
PS50011
PS00108

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0052572

response to host immune response

PMID:16585755[1]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046890

regulation of lipid biosynthetic process

PMID:16585755[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046777

protein autophosphorylation

PMID:14690440[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045926

negative regulation of growth

PMID:16077122[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0045927

positive regulation of growth

PMID:22383473[4]

ECO:0000314

P

Figure 4b. pknH is required for diazotrophic growth

complete
CACAO 9150

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

PMID:16585755[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

UniProtKB:P9WNL5

P

Seeded From UniProt

complete

involved_in

GO:0043388

positive regulation of DNA binding

PMID:16817899[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043388

positive regulation of DNA binding

PMID:16585755[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:15043876[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004674

protein serine/threonine kinase activity

PMID:15043876[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004674

protein serine/threonine kinase activity

PMID:14690440[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004672

protein kinase activity

PMID:17999640[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004672

protein kinase activity

PMID:17286964[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043086

negative regulation of catalytic activity

PMID:16873379[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043085

positive regulation of catalytic activity

PMID:16873379[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:20825248[10]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004672

protein kinase activity

PMID:16873379[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004672

protein kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000719
InterPro:IPR008271

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000719
InterPro:IPR017441

F

Seeded From UniProt

complete

involved_in

GO:0006468

protein phosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000719
InterPro:IPR008271

P

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

enables

GO:0004674

protein serine/threonine kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0723

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Sharma, K et al. (2006) Transcriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein, EmbR, in vivo. J. Bacteriol. 188 2936-44 PubMed GONUTS page
  2. 2.0 2.1 Molle, V et al. (2003) An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis. Biochemistry 42 15300-9 PubMed GONUTS page
  3. Papavinasasundaram, KG et al. (2005) Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB/c mice. J. Bacteriol. 187 5751-60 PubMed GONUTS page
  4. Ehira, S & Ohmori, M (2012) The pknH gene restrictively expressed in heterocysts is required for diazotrophic growth in the cyanobacterium Anabaena sp. strain PCC 7120. Microbiology (Reading, Engl.) 158 1437-43 PubMed GONUTS page
  5. Sharma, K et al. (2006) EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis. FEBS J. 273 2711-21 PubMed GONUTS page
  6. 6.0 6.1 Sharma, K et al. (2004) PknH, a transmembrane Hank's type serine/threonine kinase from Mycobacterium tuberculosis is differentially expressed under stress conditions. FEMS Microbiol. Lett. 233 107-13 PubMed GONUTS page
  7. Molle, V et al. (2008) EmbR2, a structural homologue of EmbR, inhibits the Mycobacterium tuberculosis kinase/substrate pair PknH/EmbR. Biochem. J. 410 309-17 PubMed GONUTS page
  8. Zheng, X et al. (2007) Novel substrates of Mycobacterium tuberculosis PknH Ser/Thr kinase. Biochem. Biophys. Res. Commun. 355 162-8 PubMed GONUTS page
  9. 9.0 9.1 9.2 Molle, V et al. (2006) The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J. Biol. Chem. 281 30094-103 PubMed GONUTS page
  10. Wolfe, LM et al. (2010) Proteomic definition of the cell wall of Mycobacterium tuberculosis. J. Proteome Res. 9 5816-26 PubMed GONUTS page