ANKX_LEGPH
ID ANKX_LEGPH Reviewed; 949 AA.
AC Q5ZXN6;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phosphocholine transferase AnkX;
DE Short=PC transferase;
DE EC=2.7.1.-;
DE AltName: Full=Ankyrin repeat-containing protein X;
GN Name=ankX; Synonyms=legA8; OrderedLocusNames=lpg0695;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2]
RP FUNCTION.
RX PubMed=18566289; DOI=10.1126/science.1158160;
RA Pan X., Luhrmann A., Satoh A., Laskowski-Arce M.A., Roy C.R.;
RT "Ankyrin repeat proteins comprise a diverse family of bacterial type IV
RT effectors.";
RL Science 320:1651-1654(2008).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22158903; DOI=10.1073/pnas.1114023109;
RA Tan Y., Arnold R.J., Luo Z.Q.;
RT "Legionella pneumophila regulates the small GTPase Rab1 activity by
RT reversible phosphorylcholination.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21212-21217(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-229.
RX PubMed=21822290; DOI=10.1038/nature10335;
RA Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R.;
RT "Modulation of Rab GTPase function by a protein phosphocholine
RT transferase.";
RL Nature 477:103-106(2011).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22307087; DOI=10.1038/emboj.2012.16;
RA Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S.;
RT "Reversible phosphocholination of Rab proteins by Legionella pneumophila
RT effector proteins.";
RL EMBO J. 31:1774-1784(2012).
RN [6]
RP FUNCTION.
RX PubMed=22411835; DOI=10.1073/pnas.1121161109;
RA Oesterlin L.K., Goody R.S., Itzen A.;
RT "Posttranslational modifications of Rab proteins cause effective
RT displacement of GDP dissociation inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5621-5626(2012).
CC -!- FUNCTION: Virulence effector that plays a role in hijacking the host
CC vesicular trafficking by recruiting the small guanosine triphosphatase
CC (GTPase) Rab1 to the cytosolic face of the Legionella-containing
CC vacuole (LCVs). Acts as a phosphocholine transferase by mediating the
CC addition of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B
CC or RAB1C) and RAB35, leading to displacement of GDP dissociation
CC inhibitors (GDI). Phosphocholination of target proteins also impairs
CC accessibility to GTPase effector LepB. Can act on both GDP-bound and
CC GTP-bound Rab proteins. {ECO:0000269|PubMed:18566289,
CC ECO:0000269|PubMed:21822290, ECO:0000269|PubMed:22158903,
CC ECO:0000269|PubMed:22307087, ECO:0000269|PubMed:22411835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Rab1 protein]-L-serine + CDP-choline = [Rab1 protein]-O-
CC phosphocholine-L-serine + CMP + H(+); Xref=Rhea:RHEA:56080,
CC Rhea:RHEA-COMP:14085, Rhea:RHEA-COMP:14376, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:58779, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:138595; Evidence={ECO:0000269|PubMed:21822290};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=122 uM for RAB1B {ECO:0000269|PubMed:22307087};
CC -!- INTERACTION:
CC Q5ZXN6; Q86WP2: GPBP1; Xeno; NbExp=2; IntAct=EBI-26359852, EBI-2349758;
CC Q5ZXN6; Q8N3F8: MICALL1; Xeno; NbExp=2; IntAct=EBI-26359852, EBI-1056885;
CC Q5ZXN6; Q9H4M7: PLEKHA4; Xeno; NbExp=2; IntAct=EBI-26359852, EBI-716549;
CC Q5ZXN6; Q494U1: PLEKHN1; Xeno; NbExp=7; IntAct=EBI-26359852, EBI-10241513;
CC Q5ZXN6; Q8TBK6: ZCCHC10; Xeno; NbExp=2; IntAct=EBI-26359852, EBI-597063;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22158903}. Host
CC cytoplasm {ECO:0000269|PubMed:22158903}. Note=Translocated into the
CC host cell via the type IV secretion system (T4SS).
CC -!- DOMAIN: The FIDO domain mediates the phosphocholine transferase
CC activity. {ECO:0000269|PubMed:21822290}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017354; AAU26784.1; -; Genomic_DNA.
DR RefSeq; WP_010946432.1; NC_002942.5.
DR RefSeq; YP_094731.1; NC_002942.5.
DR PDB; 4BEP; X-ray; 3.14 A; A/B=2-484.
DR PDB; 4BER; X-ray; 2.60 A; A/B=2-484.
DR PDB; 4BES; X-ray; 2.54 A; A=2-484.
DR PDB; 4BET; X-ray; 2.55 A; A/B=2-484.
DR PDB; 6SKU; X-ray; 3.20 A; A=1-800.
DR PDBsum; 4BEP; -.
DR PDBsum; 4BER; -.
DR PDBsum; 4BES; -.
DR PDBsum; 4BET; -.
DR PDBsum; 6SKU; -.
DR AlphaFoldDB; Q5ZXN6; -.
DR SMR; Q5ZXN6; -.
DR IntAct; Q5ZXN6; 8.
DR MINT; Q5ZXN6; -.
DR STRING; 272624.lpg0695; -.
DR PaxDb; Q5ZXN6; -.
DR PRIDE; Q5ZXN6; -.
DR EnsemblBacteria; AAU26784; AAU26784; lpg0695.
DR GeneID; 66489882; -.
DR KEGG; lpn:lpg0695; -.
DR PATRIC; fig|272624.6.peg.717; -.
DR eggNOG; COG0666; Bacteria.
DR eggNOG; COG3177; Bacteria.
DR HOGENOM; CLU_308777_0_0_6; -.
DR SABIO-RK; Q5ZXN6; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0044605; F:phosphocholine transferase activity; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR Gene3D; 1.10.3290.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF02661; Fic; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF140931; SSF140931; 1.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51459; FIDO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Host cytoplasm; Reference proteome; Repeat;
KW Secreted; Transferase; Virulence.
FT CHAIN 1..949
FT /note="Phosphocholine transferase AnkX"
FT /id="PRO_0000417543"
FT DOMAIN 155..289
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT REPEAT 391..420
FT /note="ANK 1"
FT REPEAT 424..453
FT /note="ANK 2"
FT REPEAT 464..494
FT /note="ANK 3"
FT REPEAT 498..527
FT /note="ANK 4"
FT REPEAT 554..583
FT /note="ANK 5"
FT REPEAT 588..617
FT /note="ANK 6"
FT REPEAT 658..687
FT /note="ANK 7"
FT REPEAT 691..720
FT /note="ANK 8"
FT REPEAT 725..767
FT /note="ANK 9"
FT REPEAT 771..800
FT /note="ANK 10"
FT MUTAGEN 229
FT /note="H->A: Abolishes phosphocholine transferase
FT activity."
FT /evidence="ECO:0000269|PubMed:21822290"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:4BER"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:4BES"
FT TURN 29..38
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:4BES"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4BEP"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4BET"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:4BES"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4BES"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4BES"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4BET"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:4BES"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6SKU"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 211..227
FT /evidence="ECO:0007829|PDB:4BES"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:4BES"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4BES"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 269..291
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 318..324
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:4BES"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:4BET"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:4BES"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 405..413
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 428..435
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 438..449
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 454..458
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 468..473
FT /evidence="ECO:0007829|PDB:4BES"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:4BES"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 502..508
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 512..520
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 527..536
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 539..549
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 556..564
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 568..577
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 592..598
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 602..610
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 625..628
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 634..647
FT /evidence="ECO:0007829|PDB:6SKU"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 662..668
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 672..680
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 695..699
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 706..715
FT /evidence="ECO:0007829|PDB:6SKU"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 728..734
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 743..757
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 774..781
FT /evidence="ECO:0007829|PDB:6SKU"
FT TURN 784..786
FT /evidence="ECO:0007829|PDB:6SKU"
FT HELIX 787..793
FT /evidence="ECO:0007829|PDB:6SKU"
SQ SEQUENCE 949 AA; 107151 MW; F467E4D5631800EE CRC64;
MVKIMPNLPG LYFLQAYPSE EIWRLFVDGR FWSKENGWRG YESREPGCLN AALESLCSIA
LQVEKSGEEF ELSVDLIKRI HKKCGKKVEE LQEKNPGELR TDEPVSFGIP AGRASIKGIE
EFLSLVFLTE GGAEFGPGKA GPFGPRFDKN YFKNLNPEQI PDLAKQIYFD MCKYGHSNTN
HFYLAVMKNV DVYLEKITQS YNKEIKTAET LDEKLKIIVK HIRMYEVLHP FRDANGRTFV
NNLLNILLMQ QGLPPATFYE PNVFDLYSAE ELVVVVKEAI FNTVEIIEQS KRKTPITLYG
YHSSLEEQTK FRDMLDSPSY EKIKHMDFSD LNPEKLHLKT QKCLSSLNEQ YPLHRGAIYL
SDPGEIKLLL SNRNESQINQ QIEQGAPPIY VGKTPAHLAV ISGNMAMLDE LIAKKADLSL
QDYDGKTALH YAAECGNMQI MGKILKVVLS QEDAIKVLNI KDNHGKTAFH YAAEFGTPEL
ISALTTTEVI QINEPDNSGS SAITLAYKNH KLKIFDELLN SGADISDELL DAIWARKDKE
TLGKIIAKNE KILLNKEAFR IAISLGSVSL VKKFLRAGVD IDIPLTKDKA TPLMLSINSG
NPKLVSYLLK KGANTRLTDT SGNSVLHYVF YSKAENREAL ANIITEKDKK LINQPNANGN
PPLYNAVVVN DLKMATILLE MGARVDFEDR LGNNILHSAM RRCDLPIILD IVKKDSTLLH
KRNSERRNPF HQALHEMHTF PSSKETEEIH FMNLSDLLLK EGVDLNKKDI KGKTILDIAL
SKQYFHLCVK LMKAGAHTNI SSPSKFLKNS DANSILERPF KFKNDLKKEL DNNPLIAMAQ
INDLYVQIKN NRIRTPTGYA PKEGVSFFKG KSNDAKAHDE VLSVLKELYD SKLTEMLGNL
PGEGLEEIKR SQKFFDGELK LLIKNQDISR KVDKKSIQEA VGTSLKLKW
