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Protein

Phosphocholine transferase AnkX

Gene

ankX

Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a phosphocholine transferase by mediating the addition of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B or RAB1C) and RAB35, leading to displacement of GDP dissociation inhibitors (GDI). Phosphocholination of target proteins also impairs accessibility to GTPase effector LepB. Can act on both GDP-bound and GTP-bound Rab proteins.5 Publications

Catalytic activityi

CDP-choline + protein-serine = CMP + protein-serine-choline phosphate.1 Publication

Kineticsi

  1. KM=122 µM for RAB1B1 Publication

    GO - Molecular functioni

    • phosphocholine transferase activity Source: UniProtKB

    GO - Biological processi

    • metabolic process Source: UniProtKB
    • pathogenesis Source: UniProtKB
    • regulation of GTPase activity Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Virulence

    Enzyme and pathway databases

    BioCyciLPNE272624:GHDI-694-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphocholine transferase AnkX (EC:2.7.1.-)
    Short name:
    PC transferase
    Alternative name(s):
    Ankyrin repeat-containing protein X
    Gene namesi
    Name:ankX
    Synonyms:legA8
    Ordered Locus Names:lpg0695
    OrganismiLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
    Taxonomic identifieri272624 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
    ProteomesiUP000000609 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    • host cell cytoplasm Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Host cytoplasm, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi229 – 2291H → A: Abolishes phosphocholine transferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 949949Phosphocholine transferase AnkXPRO_0000417543Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272624.lpg0695.

    Structurei

    Secondary structure

    1
    949
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 43Combined sources
    Helixi11 – 166Combined sources
    Helixi19 – 257Combined sources
    Turni29 – 3810Combined sources
    Helixi39 – 446Combined sources
    Helixi48 – 6417Combined sources
    Beta strandi66 – 694Combined sources
    Helixi74 – 8411Combined sources
    Helixi89 – 924Combined sources
    Beta strandi106 – 1094Combined sources
    Helixi111 – 1133Combined sources
    Helixi116 – 1249Combined sources
    Helixi126 – 1305Combined sources
    Beta strandi134 – 1418Combined sources
    Beta strandi144 – 1485Combined sources
    Turni151 – 1544Combined sources
    Turni157 – 1593Combined sources
    Helixi160 – 17415Combined sources
    Beta strandi181 – 1844Combined sources
    Helixi190 – 20718Combined sources
    Helixi211 – 22717Combined sources
    Beta strandi231 – 2333Combined sources
    Helixi235 – 2395Combined sources
    Turni240 – 2445Combined sources
    Helixi245 – 2506Combined sources
    Turni262 – 2654Combined sources
    Helixi269 – 29123Combined sources
    Helixi298 – 3003Combined sources
    Helixi305 – 31410Combined sources
    Helixi318 – 3247Combined sources
    Helixi333 – 34412Combined sources
    Helixi345 – 3473Combined sources
    Beta strandi348 – 3514Combined sources
    Helixi352 – 3598Combined sources
    Helixi363 – 3708Combined sources
    Helixi375 – 3784Combined sources
    Turni388 – 3903Combined sources
    Helixi395 – 4028Combined sources
    Helixi405 – 4139Combined sources
    Helixi428 – 4358Combined sources
    Helixi438 – 44912Combined sources
    Helixi454 – 4585Combined sources
    Helixi468 – 4736Combined sources
    Turni474 – 4763Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BEPX-ray3.14A/B2-484[»]
    4BERX-ray2.60A/B2-484[»]
    4BESX-ray2.54A2-484[»]
    4BETX-ray2.55A/B2-484[»]
    ProteinModelPortaliQ5ZXN6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini155 – 289135FidoPROSITE-ProRule annotationAdd
    BLAST
    Repeati391 – 42030ANK 1Add
    BLAST
    Repeati424 – 45330ANK 2Add
    BLAST
    Repeati464 – 49431ANK 3Add
    BLAST
    Repeati498 – 52730ANK 4Add
    BLAST
    Repeati554 – 58330ANK 5Add
    BLAST
    Repeati588 – 61730ANK 6Add
    BLAST
    Repeati658 – 68730ANK 7Add
    BLAST
    Repeati691 – 72030ANK 8Add
    BLAST
    Repeati725 – 76743ANK 9Add
    BLAST
    Repeati771 – 80030ANK 10Add
    BLAST

    Domaini

    The FIDO domain mediates the phosphocholine transferase activity.1 Publication

    Sequence similaritiesi

    Contains 10 ANK repeats.PROSITE-ProRule annotation
    Contains 1 fido domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000278898.
    OrthoDBiEOG6BW4TS.

    Family and domain databases

    Gene3Di1.10.3290.10. 2 hits.
    1.25.40.20. 2 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003812. Fido.
    [Graphical view]
    PfamiPF12796. Ank_2. 3 hits.
    PF02661. Fic. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 11 hits.
    [Graphical view]
    SUPFAMiSSF140931. SSF140931. 1 hit.
    SSF48403. SSF48403. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    PS51459. FIDO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5ZXN6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVKIMPNLPG LYFLQAYPSE EIWRLFVDGR FWSKENGWRG YESREPGCLN
    60 70 80 90 100
    AALESLCSIA LQVEKSGEEF ELSVDLIKRI HKKCGKKVEE LQEKNPGELR
    110 120 130 140 150
    TDEPVSFGIP AGRASIKGIE EFLSLVFLTE GGAEFGPGKA GPFGPRFDKN
    160 170 180 190 200
    YFKNLNPEQI PDLAKQIYFD MCKYGHSNTN HFYLAVMKNV DVYLEKITQS
    210 220 230 240 250
    YNKEIKTAET LDEKLKIIVK HIRMYEVLHP FRDANGRTFV NNLLNILLMQ
    260 270 280 290 300
    QGLPPATFYE PNVFDLYSAE ELVVVVKEAI FNTVEIIEQS KRKTPITLYG
    310 320 330 340 350
    YHSSLEEQTK FRDMLDSPSY EKIKHMDFSD LNPEKLHLKT QKCLSSLNEQ
    360 370 380 390 400
    YPLHRGAIYL SDPGEIKLLL SNRNESQINQ QIEQGAPPIY VGKTPAHLAV
    410 420 430 440 450
    ISGNMAMLDE LIAKKADLSL QDYDGKTALH YAAECGNMQI MGKILKVVLS
    460 470 480 490 500
    QEDAIKVLNI KDNHGKTAFH YAAEFGTPEL ISALTTTEVI QINEPDNSGS
    510 520 530 540 550
    SAITLAYKNH KLKIFDELLN SGADISDELL DAIWARKDKE TLGKIIAKNE
    560 570 580 590 600
    KILLNKEAFR IAISLGSVSL VKKFLRAGVD IDIPLTKDKA TPLMLSINSG
    610 620 630 640 650
    NPKLVSYLLK KGANTRLTDT SGNSVLHYVF YSKAENREAL ANIITEKDKK
    660 670 680 690 700
    LINQPNANGN PPLYNAVVVN DLKMATILLE MGARVDFEDR LGNNILHSAM
    710 720 730 740 750
    RRCDLPIILD IVKKDSTLLH KRNSERRNPF HQALHEMHTF PSSKETEEIH
    760 770 780 790 800
    FMNLSDLLLK EGVDLNKKDI KGKTILDIAL SKQYFHLCVK LMKAGAHTNI
    810 820 830 840 850
    SSPSKFLKNS DANSILERPF KFKNDLKKEL DNNPLIAMAQ INDLYVQIKN
    860 870 880 890 900
    NRIRTPTGYA PKEGVSFFKG KSNDAKAHDE VLSVLKELYD SKLTEMLGNL
    910 920 930 940
    PGEGLEEIKR SQKFFDGELK LLIKNQDISR KVDKKSIQEA VGTSLKLKW
    Length:949
    Mass (Da):107,151
    Last modified:November 23, 2004 - v1
    Checksum:iF467E4D5631800EE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE017354 Genomic DNA. Translation: AAU26784.1.
    RefSeqiWP_010946432.1. NC_002942.5.
    YP_094731.1. NC_002942.5.

    Genome annotation databases

    EnsemblBacteriaiAAU26784; AAU26784; lpg0695.
    GeneIDi19832260.
    KEGGilpn:lpg0695.
    PATRICi22328374. VBILegPne29832_0717.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE017354 Genomic DNA. Translation: AAU26784.1.
    RefSeqiWP_010946432.1. NC_002942.5.
    YP_094731.1. NC_002942.5.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BEPX-ray3.14A/B2-484[»]
    4BERX-ray2.60A/B2-484[»]
    4BESX-ray2.54A2-484[»]
    4BETX-ray2.55A/B2-484[»]
    ProteinModelPortaliQ5ZXN6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272624.lpg0695.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAU26784; AAU26784; lpg0695.
    GeneIDi19832260.
    KEGGilpn:lpg0695.
    PATRICi22328374. VBILegPne29832_0717.

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000278898.
    OrthoDBiEOG6BW4TS.

    Enzyme and pathway databases

    BioCyciLPNE272624:GHDI-694-MONOMER.

    Family and domain databases

    Gene3Di1.10.3290.10. 2 hits.
    1.25.40.20. 2 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003812. Fido.
    [Graphical view]
    PfamiPF12796. Ank_2. 3 hits.
    PF02661. Fic. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 11 hits.
    [Graphical view]
    SUPFAMiSSF140931. SSF140931. 1 hit.
    SSF48403. SSF48403. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    PS51459. FIDO. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Philadelphia 1 / ATCC 33152 / DSM 7513.
    2. "Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors."
      Pan X., Luhrmann A., Satoh A., Laskowski-Arce M.A., Roy C.R.
      Science 320:1651-1654(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    3. "Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination."
      Tan Y., Arnold R.J., Luo Z.Q.
      Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    4. "Modulation of Rab GTPase function by a protein phosphocholine transferase."
      Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.
      Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-229.
    5. "Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins."
      Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S.
      EMBO J. 31:1774-1784(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor."
      Oesterlin L.K., Goody R.S., Itzen A.
      Proc. Natl. Acad. Sci. U.S.A. 109:5621-5626(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiANKX_LEGPH
    AccessioniPrimary (citable) accession number: Q5ZXN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2012
    Last sequence update: November 23, 2004
    Last modified: April 29, 2015
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.