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Q5ZXN6

- ANKX_LEGPH

UniProt

Q5ZXN6 - ANKX_LEGPH

Protein

Phosphocholine transferase AnkX

Gene

ankX

Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    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

    1. phosphocholine transferase activity Source: UniProtKB

    GO - Biological processi

    1. metabolic process Source: UniProtKB
    2. pathogenesis Source: UniProtKB
    3. regulation of Rab GTPase activity Source: UniProtKB

    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: Chromosome

    Subcellular locationi

    Secreted 1 Publication. Host cytoplasm 1 Publication
    Note: Translocated into the host cell via the type IV secretion system (T4SS).

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiFWSKENG.
    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

    MVKIMPNLPG LYFLQAYPSE EIWRLFVDGR FWSKENGWRG YESREPGCLN    50
    AALESLCSIA LQVEKSGEEF ELSVDLIKRI HKKCGKKVEE LQEKNPGELR 100
    TDEPVSFGIP AGRASIKGIE EFLSLVFLTE GGAEFGPGKA GPFGPRFDKN 150
    YFKNLNPEQI PDLAKQIYFD MCKYGHSNTN HFYLAVMKNV DVYLEKITQS 200
    YNKEIKTAET LDEKLKIIVK HIRMYEVLHP FRDANGRTFV NNLLNILLMQ 250
    QGLPPATFYE PNVFDLYSAE ELVVVVKEAI FNTVEIIEQS KRKTPITLYG 300
    YHSSLEEQTK FRDMLDSPSY EKIKHMDFSD LNPEKLHLKT QKCLSSLNEQ 350
    YPLHRGAIYL SDPGEIKLLL SNRNESQINQ QIEQGAPPIY VGKTPAHLAV 400
    ISGNMAMLDE LIAKKADLSL QDYDGKTALH YAAECGNMQI MGKILKVVLS 450
    QEDAIKVLNI KDNHGKTAFH YAAEFGTPEL ISALTTTEVI QINEPDNSGS 500
    SAITLAYKNH KLKIFDELLN SGADISDELL DAIWARKDKE TLGKIIAKNE 550
    KILLNKEAFR IAISLGSVSL VKKFLRAGVD IDIPLTKDKA TPLMLSINSG 600
    NPKLVSYLLK KGANTRLTDT SGNSVLHYVF YSKAENREAL ANIITEKDKK 650
    LINQPNANGN PPLYNAVVVN DLKMATILLE MGARVDFEDR LGNNILHSAM 700
    RRCDLPIILD IVKKDSTLLH KRNSERRNPF HQALHEMHTF PSSKETEEIH 750
    FMNLSDLLLK EGVDLNKKDI KGKTILDIAL SKQYFHLCVK LMKAGAHTNI 800
    SSPSKFLKNS DANSILERPF KFKNDLKKEL DNNPLIAMAQ INDLYVQIKN 850
    NRIRTPTGYA PKEGVSFFKG KSNDAKAHDE VLSVLKELYD SKLTEMLGNL 900
    PGEGLEEIKR SQKFFDGELK LLIKNQDISR KVDKKSIQEA VGTSLKLKW 949
    Length:949
    Mass (Da):107,151
    Last modified:November 23, 2004 - v1
    Checksum:iF467E4D5631800EE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017354 Genomic DNA. Translation: AAU26784.1.
    RefSeqiYP_094731.1. NC_002942.5.

    Genome annotation databases

    EnsemblBacteriaiAAU26784; AAU26784; lpg0695.
    GeneIDi3080630.
    KEGGilpn:lpg0695.
    PATRICi22328374. VBILegPne29832_0717.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017354 Genomic DNA. Translation: AAU26784.1 .
    RefSeqi YP_094731.1. NC_002942.5.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BEP X-ray 3.14 A/B 2-484 [» ]
    4BER X-ray 2.60 A/B 2-484 [» ]
    4BES X-ray 2.54 A 2-484 [» ]
    4BET X-ray 2.55 A/B 2-484 [» ]
    ProteinModelPortali Q5ZXN6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272624.lpg0695.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAU26784 ; AAU26784 ; lpg0695 .
    GeneIDi 3080630.
    KEGGi lpn:lpg0695.
    PATRICi 22328374. VBILegPne29832_0717.

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000278898.
    OMAi FWSKENG.
    OrthoDBi EOG6BW4TS.

    Enzyme and pathway databases

    BioCyci LPNE272624:GHDI-694-MONOMER.

    Family and domain databases

    Gene3Di 1.10.3290.10. 2 hits.
    1.25.40.20. 2 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003812. Fido.
    [Graphical view ]
    Pfami PF12796. Ank_2. 3 hits.
    PF02661. Fic. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 11 hits.
    [Graphical view ]
    SUPFAMi SSF140931. SSF140931. 1 hit.
    SSF48403. SSF48403. 2 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    PS51459. FIDO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 61 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