P65726 (PKNA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase PknA
EC=2.7.11.1

Gene names

Name:	pknA
Ordered Locus Names:	Rv0015c, MT0018
ORF Names:	MTCY10H4.15c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as FtsZ, Wag31, GlmU, FhaB, PstP, EmbR and Rv1422. Shows a strong preference for Thr versus Ser as the phosphoacceptor. Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.3
Subcellular location	Cell membrane; Single-pass membrane protein Ref.10.
Induction	Expressed predominantly in exponential phase. Ref.3
Post-translational modification	Autophosphorylated. Dephosphorylated by PstP. Ref.3 Ref.4 Ref.5
Miscellaneous	Overexpression causes major growth and morphological changes that indicate defects in cell wall synthesis and possibly in cell division (Ref.3).
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE negative regulation of catalytic activity Inferred from direct assay PubMed 16873379PubMed 17068335. Source: MTBBASE negative regulation of fatty acid biosynthetic process Inferred from direct assay PubMed 20178986. Source: MTBBASE positive regulation of DNA binding Inferred from direct assay Ref.4. Source: MTBBASE positive regulation of catalytic activity Inferred from direct assay PubMed 16873379. Source: MTBBASE protein autophosphorylation Inferred from direct assay PubMed 11856348Ref.3PubMed 16256441. Source: MTBBASE regulation of cell shape Inferred from direct assay PubMed 11856348. Source: MTBBASE
Cellular_component	cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE extracellular region Inferred from direct assay PubMed 17443846. Source: MTBBASE integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 16256441. Source: MTBBASE
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay PubMed 19074144. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Serine/threonine-protein kinase PknA		PRO_0000171205
Regions
	Topological domain	1 – 339	339	Cytoplasmic Potential
	Transmembrane	340 – 360	21	Helical; Potential
	Topological domain	361 – 431	71	Extracellular Potential
	Domain	13 – 272	260	Protein kinase
	Nucleotide binding	19 – 27	9	ATP By similarity
Sites
	Active site	141	1	Proton acceptor By similarity
	Binding site	42	1	ATP By similarity
Experimental info
	Mutagenesis	42	1	K → M: Lack of autophosphorylation. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P65726 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 582D183747F3C111	FASTA	431	45,597
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape." Kang C.M., Abbott D.W., Park S.T., Dascher C.C., Cantley L.C., Husson R.N. Genes Dev. 19:1692-1704(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AUTOPHOSPHORYLATION, OVEREXPRESSION, MUTAGENESIS OF LYS-42. Strain: ATCC 25618 / H37Rv.
[4]	"EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis." Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y. FEBS J. 273:2711-2721(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH EMBR AS SUBSTRATE, DEPHOSPHORYLATION BY PSTP.
[5]	"Characterization of the phosphorylation sites of Mycobacterium tuberculosis serine/threonine protein kinases, PknA, PknD, PknE, and PknH by mass spectrometry." Molle V., Zanella-Cleon I., Robin J.P., Mallejac S., Cozzone A.J., Becchi M. Proteomics 6:3754-3766(2006) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION, MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.
[6]	"PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity." Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K. J. Mol. Biol. 386:451-464(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH GLMU AS SUBSTRATE.
[7]	"Regulation of polar peptidoglycan biosynthesis by Wag31 phosphorylation in mycobacteria." Jani C., Eoh H., Lee J.J., Hamasha K., Sahana M.B., Han J.S., Nyayapathy S., Lee J.Y., Suh J.W., Lee S.H., Rehse S.J., Crick D.C., Kang C.M. BMC Microbiol. 10:327-327(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH WAG31 AS SUBSTRATE.
[8]	"Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division." Sureka K., Hossain T., Mukherjee P., Chatterjee P., Datta P., Kundu M., Basu J. PLoS ONE 5:E8590-E8590(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH FHAB AS SUBSTRATE. Strain: ATCC 25618 / H37Rv.
[9]	"Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB." Sajid A., Arora G., Gupta M., Upadhyay S., Nandicoori V.K., Singh Y. PLoS ONE 6:E17871-E17871(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH PSTP AS SUBSTRATE. Strain: ATCC 25618 / H37Rv.
[10]	"The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization." Mir M., Asong J., Li X., Cardot J., Boons G.J., Husson R.N. PLoS Pathog. 7:E1002182-E1002182(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842572 Genomic DNA. Translation: CAB02435.1. AE000516 Genomic DNA. Translation: AAK44240.1. AL123456 Genomic DNA. Translation: CCP42737.1.
PIR	E70699.
RefSeq	NP_214529.1. NC_000962.3. NP_334426.1. NC_002755.2. YP_006513329.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P65726.
SMR	P65726. Positions 9-265.
ModBase	Search...
Protein-protein interaction databases
IntAct	P65726. 2 interactions.
STRING	83332.Rv0015c.
PTM databases
PhosSite	P12071661.
Proteomic databases
PRIDE	P65726.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK44240; AAK44240; MT0018.
GeneID	13315992. 885953. 922466.
KEGG	mtc:MT0018. mtu:Rv0015c. mtv:RVBD_0015c.
PATRIC	18121766. VBIMycTub22151_0019.
Organism-specific databases
TubercuList	Rv0015c.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000037187.
KO	K08884.
OMA	FVERFRI.
ProtClustDB	CLSK790193.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PKNA_MYCTU

Accession

Primary (citable) accession number: P65726
Secondary accession number(s): L0T594, P71585

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program