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   27-MAR-2024, entry version 101.
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; Pseudomonadota; 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}.
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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; 9.
DR   MINT; Q5ZXN6; -.
DR   STRING; 272624.lpg0695; -.
DR   PaxDb; 272624-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   OrthoDB; 5649256at2; -.
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; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003812; Fido.
DR   InterPro; IPR036597; Fido-like_dom_sf.
DR   PANTHER; PTHR24193:SF128; ANKYRIN REPEAT AND KH DOMAIN-CONTAINING PROTEIN MASK-LIKE PROTEIN; 1.
DR   PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 11.
DR   SUPFAM; SSF48403; Ankyrin repeat; 2.
DR   SUPFAM; SSF140931; Fic-like; 1.
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
//