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Q5ZXN6

- ANKX_LEGPH

UniProt

Q5ZXN6 - ANKX_LEGPH

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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: 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

  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
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: 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
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 – 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 [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:
EMBL
GenBank
DDBJ
Links Updated
AE017354 Genomic DNA. Translation: AAU26784.1.
RefSeqiYP_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:
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 19832260.
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

« 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: October 29, 2014
This is version 62 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