MYCTU:PKNF

Species (Taxon ID)	Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s)	pknF
Protein Name(s)	Serine/threonine-protein kinase PknF
External Links
UniProt	P9WI75
EMBL	AL123456
PIR	C70986
RefSeq	NP_216262.1 WP_003899000.1
ProteinModelPortal	P9WI75
SMR	P9WI75
IntAct	P9WI75
STRING	83332.Rv1746
ChEMBL	CHEMBL2016432
iPTMnet	P9WI75
PaxDb	P9WI75
EnsemblBacteria	CCP44512
GeneID	885275
KEGG	mtu:Rv1746
TubercuList	Rv1746
eggNOG	ENOG4105DWG COG0515
KO	K08884
OMA	PEIVEGH
PhylomeDB	P9WI75
PRO	PR:P9WI75
Proteomes	UP000001584
GO	GO:0005829 GO:0005887 GO:0005524 GO:0004672 GO:0004674 GO:0000917 GO:0043086 GO:0051055 GO:0043085 GO:0001558 GO:0010827
InterPro	IPR011009 IPR000719 IPR008271
Pfam	PF00069
SMART	SM00220
SUPFAM	SSF56112
PROSITE	PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0043086	negative regulation of catalytic activity	PMID:16873379^[1]	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^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:16873379^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051055	negative regulation of lipid biosynthetic process	PMID:19074144^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010827	regulation of glucose transmembrane transport	PMID:15866927^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:11496007^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:11496007^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:19201789^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:19074144^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:15978616^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:11496007^[4]	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:15987910^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:15135525^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0001558	regulation of cell growth	PMID:15866927^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000921	septin ring assembly	PMID:15866927^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	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	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
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
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
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
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: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
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
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
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 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
↑ ^2.0 ^2.1 Veyron-Churlet, R et al. (2009) The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue. J. Biol. Chem. 284 6414-24 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Deol, P et al. (2005) Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: implications in glucose transport and cell division. J. Bacteriol. 187 3415-20 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Koul, A et al. (2001) Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization. Microbiology (Reading, Engl.) 147 2307-14 PubMed GONUTS page
↑ Zhang, J et al. (2009) The core oligosaccharide and thioredoxin of Vibrio cholerae are necessary for binding and propagation of its typing phage VP3. J. Bacteriol. 191 2622-9 PubMed GONUTS page
↑ Villarino, A et al. (2005) Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions. J. Mol. Biol. 350 953-63 PubMed GONUTS page
↑ 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
↑ Grundner, C et al. (2005) Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains. Protein Sci. 14 1918-21 PubMed GONUTS page
↑ Molle, V et al. (2004) Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis. FEMS Microbiol. Lett. 234 215-23 PubMed GONUTS page

[PMID:16873379-1] 1.0 ^1.1 ^1.2 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

[PMID:19074144-2] 2.0 ^2.1 Veyron-Churlet, R et al. (2009) The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue. J. Biol. Chem. 284 6414-24 PubMed GONUTS page

[PMID:15866927-3] 3.0 ^3.1 ^3.2 Deol, P et al. (2005) Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: implications in glucose transport and cell division. J. Bacteriol. 187 3415-20 PubMed GONUTS page

[PMID:11496007-4] 4.0 ^4.1 ^4.2 Koul, A et al. (2001) Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization. Microbiology (Reading, Engl.) 147 2307-14 PubMed GONUTS page

[PMID:19201789-5] Zhang, J et al. (2009) The core oligosaccharide and thioredoxin of Vibrio cholerae are necessary for binding and propagation of its typing phage VP3. J. Bacteriol. 191 2622-9 PubMed GONUTS page

[PMID:15978616-6] Villarino, A et al. (2005) Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions. J. Mol. Biol. 350 953-63 PubMed GONUTS page

[PMID:17999640-7] 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

[PMID:15987910-8] Grundner, C et al. (2005) Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains. Protein Sci. 14 1918-21 PubMed GONUTS page

[PMID:15135525-9] Molle, V et al. (2004) Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis. FEMS Microbiol. Lett. 234 215-23 PubMed GONUTS page

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MYCTU:PKNF

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