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Protein

Lipopolysaccharide core heptose(I) kinase RfaP

Gene

rfaP

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

Kineticsi

For lipopolysaccharide kinase activity.

  1. KM=0.22 mM for ATP1 Publication
  2. KM=14.4 µM for hydrofluoric acid-treated lipopolysaccharide1 Publication

    Pathwayi: LPS core biosynthesis

    This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
    View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei1631

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • kinase activity Source: PseudoCAP
    • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC

    GO - Biological processi

    • lipopolysaccharide core region biosynthetic process Source: PseudoCAP
    • response to drug Source: PseudoCAP
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Lipopolysaccharide biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00958.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipopolysaccharide core heptose(I) kinase RfaP (EC:2.7.1.-, EC:2.7.10.2)
    Alternative name(s):
    Lipopolysaccharide kinase WaaP
    Gene namesi
    Name:rfaP
    Synonyms:waaP
    Ordered Locus Names:PA5009
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA5009.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Lack of viability.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi69K → A or R: Loss of protein-tyrosine kinase activity. 1 Publication1
    Mutagenesisi163D → A or E: Loss of protein-tyrosine kinase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003958011 – 268Lipopolysaccharide core heptose(I) kinase RfaPAdd BLAST268

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei30Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei48Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei98Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei165Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei211Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei231Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei258Phosphotyrosine; by autocatalysis1 Publication1
    Modified residuei264Phosphotyrosine; by autocatalysis1 Publication1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9HUF7.

    PTM databases

    iPTMnetiQ9HUF7.

    Interactioni

    Protein-protein interaction databases

    STRINGi208964.PA5009.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HUF7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107543. Bacteria.
    ENOG410XQAT. LUCA.
    HOGENOMiHOG000126215.
    InParanoidiQ9HUF7.
    KOiK02848.
    OMAiLGAGQEW.
    PhylomeDBiQ9HUF7.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR010440. LipoPS_kinase.
    IPR017172. Lsacc_core_hep_kinase_RfaP.
    [Graphical view]
    PfamiPF06293. Kdo. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037318. RfaP. 1 hit.
    SUPFAMiSSF56112. SSF56112. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9HUF7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRLVLEEPFK RLWNGRDPFE AVEALQGKVY RELEGRRTLR TEVDGRGYFV
    60 70 80 90 100
    KIHRGIGWGE IAKNLLTAKL PVLGARQEWQ AIRRLHEAGV ATMTAVAYGE
    110 120 130 140 150
    RGSDPARQHS FIVTEELAPT VDLEVFSQDW RERPPPPRLK RALVEAVARM
    160 170 180 190 200
    VGDMHRAGVN HRDCYICHFL LHTDKPVSAD DFRLSVIDLH RAQTRDATPK
    210 220 230 240 250
    RWRNKDLAAL YFSALDIGLT RRDKLRFLRT YFRRPLREIL RDEAGLLAWM
    260
    ERKAEKLYER KQRYGDLL
    Length:268
    Mass (Da):31,311
    Last modified:March 1, 2001 - v1
    Checksum:i248E8D96C78A7791
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti253K → Q in AAD12056 (PubMed:11741974).Curated1

    Mass spectrometryi

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF087652 Genomic DNA. Translation: AAD12056.1.
    AE004091 Genomic DNA. Translation: AAG08394.1.
    PIRiE83020.
    RefSeqiNP_253696.1. NC_002516.2.
    WP_003114553.1. NZ_ASJY01000797.1.

    Genome annotation databases

    EnsemblBacteriaiAAG08394; AAG08394; PA5009.
    GeneIDi881540.
    KEGGipae:PA5009.
    PATRICi19844841. VBIPseAer58763_5249.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF087652 Genomic DNA. Translation: AAD12056.1.
    AE004091 Genomic DNA. Translation: AAG08394.1.
    PIRiE83020.
    RefSeqiNP_253696.1. NC_002516.2.
    WP_003114553.1. NZ_ASJY01000797.1.

    3D structure databases

    ProteinModelPortaliQ9HUF7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA5009.

    PTM databases

    iPTMnetiQ9HUF7.

    Proteomic databases

    PaxDbiQ9HUF7.

    Protocols and materials databases

    DNASUi881540.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG08394; AAG08394; PA5009.
    GeneIDi881540.
    KEGGipae:PA5009.
    PATRICi19844841. VBIPseAer58763_5249.

    Organism-specific databases

    PseudoCAPiPA5009.

    Phylogenomic databases

    eggNOGiENOG4107543. Bacteria.
    ENOG410XQAT. LUCA.
    HOGENOMiHOG000126215.
    InParanoidiQ9HUF7.
    KOiK02848.
    OMAiLGAGQEW.
    PhylomeDBiQ9HUF7.

    Enzyme and pathway databases

    UniPathwayiUPA00958.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR010440. LipoPS_kinase.
    IPR017172. Lsacc_core_hep_kinase_RfaP.
    [Graphical view]
    PfamiPF06293. Kdo. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037318. RfaP. 1 hit.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRFAP_PSEAE
    AccessioniPrimary (citable) accession number: Q9HUF7
    Secondary accession number(s): Q9R883
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: March 1, 2001
    Last modified: November 2, 2016
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.