Serine/threonine-protein kinase PknI - Mycobacterium tuberculosis

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P65730 (PKNI_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:	pknI
Ordered Locus Names:	Rv2914c, MT2982
ORF Names:	MTCY338.02c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	585 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in slowing down the growth of mycobacteria within the infected host. Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.3 Ref.4
Cofactor	Manganese. Ref.3
Subcellular location	Cytoplasm. Cell membrane; Single-pass membrane protein. Note: More abundant in the cytosol than in the cell membrane. Ref.4
Induction	Expression decreases during infection of human macrophages. Ref.4
Post-translational modification	Autophosphorylated at serine and threonine residues. Ref.3 Ref.4
Disruption phenotype	Mutants show increased growth within macrophages and a hypervirulence phenotype in severe combined immunodeficiency mice. Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Sequence caution	The sequence AAK47308.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-serine phosphorylation Inferred from direct assay Ref.3. Source: MTBBASE peptidyl-threonine phosphorylation Inferred from direct assay Ref.3. Source: MTBBASE protein autophosphorylation Inferred from direct assay Ref.3 Ref.4. Source: MTBBASE regulation of growth rate Inferred from direct assay Ref.5. Source: MTBBASE
Cellular_component	cytosol Inferred from direct assay Ref.4. Source: MTBBASE integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from direct assay Ref.3. Source: MTBBASE protein kinase activity Inferred from direct assay Ref.3 Ref.4. Source: MTBBASE protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 585

585

Serine/threonine-protein kinase PknI

PRO_0000171220

Regions

Topological domain

1 – 349

349

Cytoplasmic Potential

Transmembrane

350 – 370

Helical; Potential

Topological domain

371 – 585

215

Extracellular Potential

Domain

12 – 252

241

Protein kinase

Nucleotide binding

18 – 26

ATP By similarity

Sites

Active site

137

Proton acceptor By similarity

Binding site

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P65730 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E52EACFF4A69C3EC
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FASTA

585

61,805

        10         20         30         40         50         60 
MALASGVTFA GYTVVRMLGC SAMGEVYLVQ HPGFPGWQAL KVLSPAMAAD DEFRRRFQRE 

        70         80         90        100        110        120 
TEVAARLFHP HILEVHDRGE FDGQLWIAMD YVDGIDATQH MADRFPAVLP VGEVLAIVTA 

       130        140        150        160        170        180 
VAGALDYAHQ RGLLHRDVNP ANVVLTSQSA GDQRILLADF GIASQPSYPA PELSAGADVD 

       190        200        210        220        230        240 
GRADQYALAL TAIHLFAGAP PVDRSHTGPL QPPKLSAFRP DLARLDGVLS RALATAPADR 

       250        260        270        280        290        300 
FGSCREFADA MNEQAGVAIA DQSSGGVDAS EVTAAAGEEA YVVDYPAYGW PEAVDCKEPS 

       310        320        330        340        350        360 
ARAPAPAAPT PQRRGSMLQS AAGVLARRLD NFSTATKAPA SPTRRRPRRI LVGAVAVLLL 

       370        380        390        400        410        420 
AGLFAVGIVI GRKTNTTATE VARPPTSGSA VPSAPTTTVA VTAPVPLDGT YRIEIQRSKQ 

       430        440        450        460        470        480 
TYDYTPTPQP PDVNTWWAFR TSCTPTECLA AATMLDDNDH TQAKTPPVRP FLMQFGEGQW 

       490        500        510        520        530        540 
KSRPETVQFP CVGPNGSPST QATTQLLALR PQPQGDLVGE MVVTVHSNEC GQQGAVIRIP 

       550        560        570        580 
AVASRSGDLP PAVTVPDPAT IPDTPDTTST ATLTPPTTTA PGPGR

« Hide

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. 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. 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]	"Cloning, overexpression, and characterization of a serine/threonine protein kinase pknI from Mycobacterium tuberculosis H37Rv." Gopalaswamy R., Narayanan P.R., Narayanan S. Protein Expr. Purif. 36:82-89(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, AUTOPHOSPHORYLATION. Strain: ATCC 25618 / H37Rv.
[4]	"Protein kinase I of Mycobacterium tuberculosis: cellular localization and expression during infection of macrophage-like cells." Singh A., Singh Y., Pine R., Shi L., Chandra R., Drlica K. Tuberculosis 86:28-33(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AUTOPHOSPHORYLATION. Strain: ATCC 25618 / H37Rv.
[5]	"The serine/threonine protein kinase PknI controls the growth of Mycobacterium tuberculosis upon infection." Gopalaswamy R., Narayanan S., Chen B., Jacobs W.R., Av-Gay Y. FEMS Microbiol. Lett. 295:23-29(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN VIRULENCE, DISRUPTION PHENOTYPE. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842581 Genomic DNA. Translation: CAA98986.1. AE000516 Genomic DNA. Translation: AAK47308.1. Different initiation. AL123456 Genomic DNA. Translation: CCP45716.1.
PIR	B70747.
RefSeq	NP_217430.1. NC_000962.3. NP_337494.1. NC_002755.2. YP_006516367.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P65730.
SMR	P65730. Positions 12-253.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv2914c.
Proteomic databases
PRIDE	P65730.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK47308; AAK47308; MT2982.
GeneID	13317707. 887642. 925293.
KEGG	mtc:MT2982. mtu:Rv2914c. mtv:RVBD_2914c.
PATRIC	18128324. VBIMycTub22151_3261.
Organism-specific databases
TubercuList	Rv2914c.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000047111.
KO	K08884.
OMA	NILLTHP.
ProtClustDB	CLSK792157.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. [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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PKNI_MYCTU

Accession

Primary (citable) accession number: P65730
Secondary accession number(s): L0TB90, Q10964

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents