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P65732 (PKNJ_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PknJ
EC=2.7.11.1
Gene names
Name:pknJ
Ordered Locus Names:Rv2088, MT2149
ORF Names:MTCY49.28
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In vitro, phosphorylates various substates such as EmbR, PepE, MmaA4, Pyk, LldD and GroEL2. Ref.3 Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3 Ref.4

Enzyme regulation

Activated by certain divalent metal cations, such as cobalt, manganese, nickel or magnesium. Zinc or iron ions do not affect activity. Ref.4

Subunit structure

Homodimer. Ref.3 Ref.4

Subcellular location

Cell membrane; Single-pass membrane protein Ref.3.

Post-translational modification

Autophosphorylated. Dephosphorylated by PstP. Ref.3 Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Serine/threonine-protein kinase PknJ
PRO_0000171222

Regions

Topological domain1 – 342342Cytoplasmic Potential
Transmembrane343 – 36321Helical; Potential
Topological domain364 – 589226Extracellular Potential
Domain14 – 276263Protein kinase
Nucleotide binding20 – 289ATP By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site431ATP By similarity

Amino acid modifications

Modified residue1681Phosphothreonine; by autocatalysis Ref.3
Modified residue1711Phosphothreonine; by autocatalysis Ref.3
Modified residue1731Phosphothreonine; by autocatalysis Ref.3
Modified residue1791Phosphothreonine; by autocatalysis Probable

Experimental info

Mutagenesis431K → A: Lack of kinase activity. Ref.4
Mutagenesis781H → A: Lack of phosphorylation. Ref.4
Mutagenesis1681T → A: Does not affect phosphorylation. Lack of phosphorylation; when associated with A-171 and A-173. Ref.3 Ref.4
Mutagenesis1711T → A: Lack of phosphorylation; when associated with A-168 and A-173. Ref.3
Mutagenesis1721S → A: Does not affect phosphorylation. Ref.4
Mutagenesis1731T → A: Lack of phosphorylation; when associated with A-168 and A-171. Ref.3
Mutagenesis1791T → A: Decreases phosphorylation. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P65732 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E1E179150E2D348E

FASTA58961,595
        10         20         30         40         50         60 
MAHELSAGSV FAGYRIERML GAGGMGTVYL ARNPDLPRSE ALKVLAAELS RDLDFRARFV 

        70         80         90        100        110        120 
READVAAGLD HPNIVAVHQR GQFEGRLWIA MQFVDGGNAE DALRAATMTT ARAVYVIGEV 

       130        140        150        160        170        180 
AKALDYAHQQ GVIHRDIKPA NFLLSRAAGG DERVLLSDFG IARALGDTGL TSTGSVLATL 

       190        200        210        220        230        240 
AYAAPEVLAG QGFDGRADLY SLGCALFRLL TGEAPFAAGA GAAVAVVAGH LHQPPPTVSD 

       250        260        270        280        290        300 
RVPGLSAAMD AVIATAMAKD PMRRFTSAGE FAHAAAAALY GGATDGWVPP SPAPHVISQG 

       310        320        330        340        350        360 
AVPGSPWWQH PVGSVTALAT PPGHGWPPGL PPLPRRPRRY RRGVAAVAAV MVVAAAAVTA 

       370        380        390        400        410        420 
VTMTSHQPRT ATPPSAAALS PTSSSTTPPQ PPIVTRSRLP GLLPPLDDVK NFVGIQNLVA 

       430        440        450        460        470        480 
HEPMLQPQTP NGSINPAECW PAVGGGVPSA YDLGTVIGFY GLTIDEPPTG TAPNQVGQLI 

       490        500        510        520        530        540 
VAFRDAATAQ RHLADLASIW RRCGGRTVTL FRSEWRRPVE LSTSVPEVVD GITTMVLTAQ 

       550        560        570        580 
GPVLRVREDH AIAAKNNVLV DVDIMTPDTS RGQQAVIGIT NYILAKIPG

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional characterization of the Mycobacterium tuberculosis serine/threonine kinase PknJ."
Jang J., Stella A., Boudou F., Levillain F., Darthuy E., Vaubourgeix J., Wang C., Bardou F., Puzo G., Gilleron M., Burlet-Schiltz O., Monsarrat B., Brodin P., Gicquel B., Neyrolles O.
Microbiology 156:1619-1631(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, PHOSPHORYLATION AT THR-168; THR-171 AND THR-173, MASS SPECTROMETRY, MUTAGENESIS OF THR-168; THR-171 AND THR-173.
Strain: ATCC 25618 / H37Rv and CDC 1551 / Oshkosh.
[4]"Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A."
Arora G., Sajid A., Gupta M., Bhaduri A., Kumar P., Basu-Modak S., Singh Y.
PLoS ONE 5:E10772-E10772(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, PHOSPHORYLATION AT THR-179, DEPHOSPHORYLATION, MUTAGENESIS OF LYS-43; HIS-78; THR-168; SER-172 AND THR-179.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000516 Genomic DNA. Translation: AAK46430.1.
AL123456 Genomic DNA. Translation: CCP44863.1.
PIRC70767.
RefSeqNP_216604.1. NC_000962.3.
NP_336616.1. NC_002755.2.
YP_006515503.1. NC_018143.1.

3D structure databases

ProteinModelPortalP65732.
SMRP65732. Positions 4-340.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2088.

PTM databases

PhosSiteP1011989.

Proteomic databases

PRIDEP65732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK46430; AAK46430; MT2149.
GeneID13316894.
888322.
924580.
KEGGmtc:MT2149.
mtu:Rv2088.
PATRIC18126488. VBIMycTub22151_2357.

Organism-specific databases

TubercuListRv2088.

Phylogenomic databases

eggNOGCOG0515.
KOK08884.
OMAARHTEDN.
ProtClustDBCLSK791619.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR026954. PknH-like_Extracell.
IPR000719. Prot_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF14032. PknH_C. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePKNJ_MYCTU
AccessionPrimary (citable) accession number: P65732
Secondary accession number(s): L0T8S8, Q10697
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 29, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents