Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9HUF7 (RFAP_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. 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

Names and origin

Protein namesRecommended name:
Lipopolysaccharide core heptose(I) kinase RfaP

EC=2.7.1.-
EC=2.7.10.2
Alternative name(s):
Lipopolysaccharide kinase WaaP
Gene names
Name:rfaP
Synonyms:waaP
Ordered Locus Names:PA5009
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core. The phosphorylation of the lipopolysaccharide core seems to occur prior to translocation to the periplasm and attachment of O-antigen. Also has protein-tyrosine kinase activity: autophosphorylates on all Tyr residues; in vitro can phosphorylate poly(Glu,Tyr). Ref.1

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Magnesium By similarity.

Pathway

Bacterial outer membrane biogenesis; LPS core biosynthesis.

Subcellular location

Cytoplasm Ref.1.

Disruption phenotype

Lack of viability. Ref.1

Miscellaneous

Shares similarity with eukaryotic protein kinases in the conserved tyrosine kinase functional motifs.

Sequence similarities

Belongs to the protein kinase superfamily. KdkA/RfaP family.

Biophysicochemical properties

Kinetic parameters:

For lipopolysaccharide kinase activity.

KM=0.22 mM for ATP Ref.1

KM=14.4 µM for hydrofluoric acid-treated lipopolysaccharide

Mass spectrometry

Molecular mass is 33544.618 Da from positions 1 - 268. Determined by MALDI. Phosphorylated protein. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268Lipopolysaccharide core heptose(I) kinase RfaP
PRO_0000395801

Sites

Active site1631

Amino acid modifications

Modified residue301Phosphotyrosine; by autocatalysis Ref.1
Modified residue481Phosphotyrosine; by autocatalysis Ref.1
Modified residue981Phosphotyrosine; by autocatalysis Ref.1
Modified residue1651Phosphotyrosine; by autocatalysis Ref.1
Modified residue2111Phosphotyrosine; by autocatalysis Ref.1
Modified residue2311Phosphotyrosine; by autocatalysis Ref.1
Modified residue2581Phosphotyrosine; by autocatalysis Ref.1
Modified residue2641Phosphotyrosine; by autocatalysis Ref.1

Experimental info

Mutagenesis691K → A or R: Loss of protein-tyrosine kinase activity. Ref.1
Mutagenesis1631D → A or E: Loss of protein-tyrosine kinase activity. Ref.1
Sequence conflict2531K → Q in AAD12056. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9HUF7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 248E8D96C78A7791

FASTA26831,311
        10         20         30         40         50         60 
MRLVLEEPFK RLWNGRDPFE AVEALQGKVY RELEGRRTLR TEVDGRGYFV KIHRGIGWGE 

        70         80         90        100        110        120 
IAKNLLTAKL PVLGARQEWQ AIRRLHEAGV ATMTAVAYGE RGSDPARQHS FIVTEELAPT 

       130        140        150        160        170        180 
VDLEVFSQDW RERPPPPRLK RALVEAVARM VGDMHRAGVN HRDCYICHFL LHTDKPVSAD 

       190        200        210        220        230        240 
DFRLSVIDLH RAQTRDATPK RWRNKDLAAL YFSALDIGLT RRDKLRFLRT YFRRPLREIL 

       250        260 
RDEAGLLAWM ERKAEKLYER KQRYGDLL 

« Hide

References

« Hide 'large scale' references
[1]"WaaP of Pseudomonas aeruginosa is a novel eukaryotic type protein-tyrosine kinase as well as a sugar kinase essential for the biosynthesis of core lipopolysaccharide."
Zhao X., Lam J.S.
J. Biol. Chem. 277:4722-4730(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 12-36; 38-54; 84-101; 151-171; 211-237 AND 257-268, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS SPECTROMETRY, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT TYR-30; TYR-48; TYR-98; TYR-165; TYR-211; TYR-231; TYR-258 AND TYR-264, MUTAGENESIS OF LYS-69 AND ASP-163.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087652 Genomic DNA. Translation: AAD12056.1.
AE004091 Genomic DNA. Translation: AAG08394.1.
PIRE83020.
RefSeqNP_253696.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9HUF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5009.

Protocols and materials databases

DNASU881540.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG08394; AAG08394; PA5009.
GeneID881540.
KEGGpae:PA5009.
PATRIC19844841. VBIPseAer58763_5249.

Organism-specific databases

PseudoCAPPA5009.

Phylogenomic databases

eggNOGNOG04355.
HOGENOMHOG000126215.
KOK02848.
OMALGAGQEW.
OrthoDBEOG63JR6W.
PhylomeDBQ9HUF7.

Enzyme and pathway databases

UniPathwayUPA00958.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR010440. LipoPS_kinase.
IPR017172. Lsacc_core_hep_kinase_RfaP.
[Graphical view]
PfamPF06293. Kdo. 1 hit.
[Graphical view]
PIRSFPIRSF037318. RfaP. 1 hit.
SUPFAMSSF56112. SSF56112. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRFAP_PSEAE
AccessionPrimary (citable) accession number: Q9HUF7
Secondary accession number(s): Q9R883
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 86 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

PATHWAY comments

Index of metabolic and biosynthesis pathways