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Q5ZXN6 (ANKX_LEGPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphocholine transferase AnkX

Short name=PC transferase
EC=2.7.1.-
Alternative name(s):
Ankyrin repeat-containing protein X
Gene names
Name:ankX
Synonyms:legA8
Ordered Locus Names:lpg0695
OrganismLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]
Taxonomic identifier272624 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length949 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6

Catalytic activity

CDP-choline + protein-serine = CMP + protein-serine-choline phosphate. Ref.4

Subcellular location

Secreted. Host cytoplasm. Note: Translocated into the host cell via the type IV secretion system (T4SS). Ref.3

Domain

The FIDO domain mediates the phosphocholine transferase activity (Ref.4).

Sequence similarities

Contains 10 ANK repeats.

Contains 1 fido domain.

Biophysicochemical properties

Kinetic parameters:

KM=122 µM for RAB1B Ref.5

Ontologies

Keywords
   Biological processVirulence
   Cellular componentHost cytoplasm
Secreted
   DomainANK repeat
Repeat
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

pathogenesis

Inferred from direct assay Ref.4Ref.3. Source: UniProtKB

regulation of Rab GTPase activity

Inferred from direct assay Ref.4Ref.3. Source: UniProtKB

   Cellular_componenthost cell cytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionphosphocholine transferase activity

Inferred from direct assay Ref.4Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 949949Phosphocholine transferase AnkX
PRO_0000417543

Regions

Domain155 – 289135Fido
Repeat391 – 42030ANK 1
Repeat424 – 45330ANK 2
Repeat464 – 49431ANK 3
Repeat498 – 52730ANK 4
Repeat554 – 58330ANK 5
Repeat588 – 61730ANK 6
Repeat658 – 68730ANK 7
Repeat691 – 72030ANK 8
Repeat725 – 76743ANK 9
Repeat771 – 80030ANK 10

Experimental info

Mutagenesis2291H → A: Abolishes phosphocholine transferase activity. Ref.4

Secondary structure

................................................................................. 949
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5ZXN6 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: F467E4D5631800EE

FASTA949107,151
        10         20         30         40         50         60 
MVKIMPNLPG LYFLQAYPSE EIWRLFVDGR FWSKENGWRG YESREPGCLN AALESLCSIA 

        70         80         90        100        110        120 
LQVEKSGEEF ELSVDLIKRI HKKCGKKVEE LQEKNPGELR TDEPVSFGIP AGRASIKGIE 

       130        140        150        160        170        180 
EFLSLVFLTE GGAEFGPGKA GPFGPRFDKN YFKNLNPEQI PDLAKQIYFD MCKYGHSNTN 

       190        200        210        220        230        240 
HFYLAVMKNV DVYLEKITQS YNKEIKTAET LDEKLKIIVK HIRMYEVLHP FRDANGRTFV 

       250        260        270        280        290        300 
NNLLNILLMQ QGLPPATFYE PNVFDLYSAE ELVVVVKEAI FNTVEIIEQS KRKTPITLYG 

       310        320        330        340        350        360 
YHSSLEEQTK FRDMLDSPSY EKIKHMDFSD LNPEKLHLKT QKCLSSLNEQ YPLHRGAIYL 

       370        380        390        400        410        420 
SDPGEIKLLL SNRNESQINQ QIEQGAPPIY VGKTPAHLAV ISGNMAMLDE LIAKKADLSL 

       430        440        450        460        470        480 
QDYDGKTALH YAAECGNMQI MGKILKVVLS QEDAIKVLNI KDNHGKTAFH YAAEFGTPEL 

       490        500        510        520        530        540 
ISALTTTEVI QINEPDNSGS SAITLAYKNH KLKIFDELLN SGADISDELL DAIWARKDKE 

       550        560        570        580        590        600 
TLGKIIAKNE KILLNKEAFR IAISLGSVSL VKKFLRAGVD IDIPLTKDKA TPLMLSINSG 

       610        620        630        640        650        660 
NPKLVSYLLK KGANTRLTDT SGNSVLHYVF YSKAENREAL ANIITEKDKK LINQPNANGN 

       670        680        690        700        710        720 
PPLYNAVVVN DLKMATILLE MGARVDFEDR LGNNILHSAM RRCDLPIILD IVKKDSTLLH 

       730        740        750        760        770        780 
KRNSERRNPF HQALHEMHTF PSSKETEEIH FMNLSDLLLK EGVDLNKKDI KGKTILDIAL 

       790        800        810        820        830        840 
SKQYFHLCVK LMKAGAHTNI SSPSKFLKNS DANSILERPF KFKNDLKKEL DNNPLIAMAQ 

       850        860        870        880        890        900 
INDLYVQIKN NRIRTPTGYA PKEGVSFFKG KSNDAKAHDE VLSVLKELYD SKLTEMLGNL 

       910        920        930        940 
PGEGLEEIKR SQKFFDGELK LLIKNQDISR KVDKKSIQEA VGTSLKLKW 

« Hide

References

« Hide 'large scale' references
[1]"The genomic sequence of the accidental pathogen Legionella pneumophila."
Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S. expand/collapse author list , Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., Russo J.J.
Science 305:1966-1968(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017354 Genomic DNA. Translation: AAU26784.1.
RefSeqYP_094731.1. NC_002942.5.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BEPX-ray3.14A/B2-484[»]
4BERX-ray2.60A/B2-484[»]
4BESX-ray2.54A2-484[»]
4BETX-ray2.55A/B2-484[»]
ProteinModelPortalQ5ZXN6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272624.lpg0695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU26784; AAU26784; lpg0695.
GeneID3080630.
KEGGlpn:lpg0695.
PATRIC22328374. VBILegPne29832_0717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000278898.
OMAFWSKENG.
OrthoDBEOG6BW4TS.

Enzyme and pathway databases

BioCycLPNE272624:GHDI-694-MONOMER.

Family and domain databases

Gene3D1.10.3290.10. 2 hits.
1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR003812. Fido.
[Graphical view]
PfamPF12796. Ank_2. 3 hits.
PF02661. Fic. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 11 hits.
[Graphical view]
SUPFAMSSF140931. SSF140931. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS51459. FIDO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANKX_LEGPH
AccessionPrimary (citable) accession number: Q5ZXN6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references