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A0QNG1 (PKNB_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PknB

EC=2.7.11.1
Gene names
Name:pknB
Ordered Locus Names:MSMEG_0028, MSMEI_0031
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. Probably phosphorylates RseA. Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

By K-252a Probable. Ref.4

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Single-pass membrane protein Potential.

Domain

The PASTA domains interact with peptidoglycans and are required for PknB localization By similarity.

Post-translational modification

Autophosphorylated. Dephosphorylated by PstP By similarity.

Disruption phenotype

When depleted (with anti-sense RNA) no vancomycin-induced degradation of RseA is seen. Ref.4

Sequence similarities

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

Contains 4 PASTA domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 625625Serine/threonine-protein kinase PknB
PRO_0000422953

Regions

Topological domain1 – 331331Cytoplasmic Potential
Transmembrane332 – 35221Helical; Potential
Topological domain353 – 625273Extracellular Potential
Domain11 – 274264Protein kinase
Domain355 – 42167PASTA 1
Domain422 – 48968PASTA 2
Domain490 – 55667PASTA 3
Domain557 – 62569PASTA 4
Nucleotide binding17 – 259ATP By similarity
Nucleotide binding93 – 953ATP By similarity
Nucleotide binding140 – 1434ATP By similarity

Sites

Active site1381Proton acceptor By similarity
Metal binding1431Magnesium By similarity
Metal binding1561Magnesium By similarity
Binding site401ATP By similarity
Binding site1561ATP By similarity

Amino acid modifications

Modified residue1691Phosphoserine; by autocatalysis By similarity
Modified residue1711Phosphothreonine; by autocatalysis By similarity
Modified residue1731Phosphothreonine; by autocatalysis By similarity
Modified residue2941Phosphothreonine; by autocatalysis By similarity
Modified residue2951Phosphoserine; by autocatalysis By similarity
Modified residue3091Phosphothreonine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QNG1 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: E9B75950ADF718DA

FASTA62566,318
        10         20         30         40         50         60 
MTTPQHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA 

        70         80         90        100        110        120 
QNAAALNHPA IVAVYDTGEA ETPNGPLPYI VMEYVDGVTL RDIVHTDGPI APRRAIEIIA 

       130        140        150        160        170        180 
DACQALNFSH QHGIIHRDVK PANIMISKNN AVKVMDFGIA RALADTGNSV TQTAAVIGTA 

       190        200        210        220        230        240 
QYLSPEQARG ETVDARSDVY SLGCVLYEIL TGEPPFIGDS PVAVAYQHVR EDPVPPSRRH 

       250        260        270        280        290        300 
ADVTPELDAV VLKALAKNPD NRYQTAAEMR ADLIRVHEGQ APDAPKVLTD AERTSMLAAP 

       310        320        330        340        350        360 
PADRAGAATQ DMPVPRPAGY SKQRSTSVAR WLIAVAVLAV LTVVVTVAIN MVGGNPRNVQ 

       370        380        390        400        410        420 
VPDVAEQSAD DAQAALQNRG FKTVIDRQPD NEVPPGLVIG TDPEAGSELG AGEQVTINVS 

       430        440        450        460        470        480 
TGPEQALVPD VAGLTPTQAR QKLKDAGFEK FRESPSPSTP EQKGRVLATN PQANQTAAII 

       490        500        510        520        530        540 
NEITIVVGAG PEDAPVLSCA GQNAESCKAI LAAGGFTNTV VVEVDNPAAA GQVVGTEPAD 

       550        560        570        580        590        600 
GQSVPKDTVI QIRVSKGNQF VMPDLVGQFW SDAYPRLTAL GWTGVLDKGP DVRDSGQRTN 

       610        620 
AVVTQSPSAG TPVNKDAKIT LSFAA 

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis."
Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.
Mol. Microbiol. 75:592-606(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE FUNCTION AS A KINASE WITH RSEA AS A SUBSTRATE, ENZYME REGULATION, DISRUPTION PHENOTYPE.
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK74027.1.
CP001663 Genomic DNA. Translation: AFP36514.1.
RefSeqYP_006564809.1. NC_018289.1.
YP_884449.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QNG1.
SMRA0QNG1. Positions 1-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_0028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK74027; ABK74027; MSMEG_0028.
AFP36514; AFP36514; MSMEI_0031.
GeneID4536298.
KEGGmsg:MSMEI_0031.
msm:MSMEG_0028.
PATRIC18072526. VBIMycSme59918_0027.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000037185.
KOK08884.
OMAMSKNPAN.
OrthoDBEOG6B35XT.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-29-MONOMER.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR005543. PASTA.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePKNB_MYCS2
AccessionPrimary (citable) accession number: A0QNG1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families