Lipopolysaccharide core heptose(I) kinase RfaP - Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

Contribute

Read comments (?) or add your own

Q9HUF7 (RFAP_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

to top of page

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

to top of page

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

Names and origin

Protein names

Recommended 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

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Protein existence	Evidence 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. K_M=0.22 mM for ATP Ref.1 K_M=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

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipopolysaccharide core region biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

268

Lipopolysaccharide core heptose(I) kinase RfaP

PRO_0000395801

Sites

Active site

1

Amino acid modifications

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Modified residue

1

Phosphotyrosine; by autocatalysis Ref.1

Experimental info

Mutagenesis

1

K → A or R: Loss of protein-tyrosine kinase activity. Ref.1

Mutagenesis

1

D → A or E: Loss of protein-tyrosine kinase activity. Ref.1

Sequence conflict

1

K → Q in AAD12056. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9HUF7 [UniParc].

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

268

31,311

        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

References

	« Hide 'large scale' referencesShow '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. 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.
PIR	E83020.
RefSeq	NP_253696.1. NC_002516.2.
3D structure databases
ProteinModelPortal	Q9HUF7.
ModBase	Search...
Protein-protein interaction databases
STRING	208964.PA5009.
Protocols and materials databases
DNASU	881540.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	881540.
KEGG	pae:PA5009.
PATRIC	19844841. VBIPseAer58763_5249.
Organism-specific databases
PseudoCAP	PA5009.
Phylogenomic databases
eggNOG	NOG04355.
HOGENOM	HOG000126215.
KO	K02848.
OMA	GVPTMTA.
ProtClustDB	PRK15123.
Enzyme and pathway databases
UniPathway	UPA00958.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR010440. LipoPS_kinase. IPR017172. Lsacc_core_hep_kinase_RfaP. [Graphical view]
Pfam	PF06293. Kdo. 1 hit. [Graphical view]
PIRSF	PIRSF037318. RfaP. 1 hit.
SUPFAM	SSF56112. Kinase_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RFAP_PSEAE

Accession

Primary (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:	May 1, 2013
This is version 78 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of page

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