ID   LEM3_LEGPH              Reviewed;         570 AA.
AC   Q5ZXN5;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Phosphocholine hydrolase Lem3;
DE            EC=3.1.3.-;
DE   AltName: Full=Dephosphocholinase Lem3;
GN   Name=lem3; OrderedLocusNames=lpg0696;
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, CATALYTIC ACTIVITY, 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   [3]
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   [4]
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 hydrolase by mediating the
CC       hydrolysis of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B
CC       or RAB1C). Dephosphocholination of target proteins restores
CC       accessibility to GTPase effector LepB. Can act on both GDP-bound and
CC       GTP-bound Rab proteins. {ECO:0000269|PubMed:22158903,
CC       ECO:0000269|PubMed:22307087, ECO:0000269|PubMed:22411835}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[Rab1 protein]-O-phosphocholine-L-serine + H2O = [Rab1
CC         protein]-L-serine + H(+) + phosphocholine; Xref=Rhea:RHEA:56084,
CC         Rhea:RHEA-COMP:14085, Rhea:RHEA-COMP:14376, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:138595,
CC         ChEBI:CHEBI:295975; Evidence={ECO:0000269|PubMed:22158903};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=65.5 uM for GDP-bound RAB1B {ECO:0000269|PubMed:22307087};
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).
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DR   EMBL; AE017354; AAU26785.1; -; Genomic_DNA.
DR   RefSeq; WP_010946433.1; NC_002942.5.
DR   RefSeq; YP_094732.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZXN5; -.
DR   STRING; 272624.lpg0696; -.
DR   PaxDb; Q5ZXN5; -.
DR   PRIDE; Q5ZXN5; -.
DR   EnsemblBacteria; AAU26785; AAU26785; lpg0696.
DR   GeneID; 66489883; -.
DR   KEGG; lpn:lpg0696; -.
DR   PATRIC; fig|272624.6.peg.718; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_514617_0_0_6; -.
DR   SABIO-RK; Q5ZXN5; -.
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:0044606; F:phosphocholine hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   SUPFAM; SSF81606; SSF81606; 1.
PE   1: Evidence at protein level;
KW   Host cytoplasm; Hydrolase; Reference proteome; Secreted; Virulence.
FT   CHAIN           1..570
FT                   /note="Phosphocholine hydrolase Lem3"
FT                   /id="PRO_0000417546"
SQ   SEQUENCE   570 AA;  64738 MW;  9EB1F5D37335E8A7 CRC64;
     MKLRYIINEN KLVFTSCNMR DKIITGKKII FSQSVAKDQT KNLSSFLSER FYSVNQSHNH
     SIIIGSSLSH QENDIEHDTI LDTSGVLVTT DTNGIVNGAR VAITDGLGGG NGDQEEDDEI
     YRVSHSSCEN FLNCDQNIDT TLSLITQPKA SDKKQTAPKT LQHTEASMAA FIYQNHPGKG
     YIGEFANIGD GLIIILDKRF KIKHMVSACH IYRGFGTWTP PSLQALATTA NKDALLVRQT
     LKLAEGDIII SMTDGVWGEL KTSLIAQTND RRDIGVDKEY FKTLFDELTD APYPSSFDIA
     RIITQRAMSR SLERRKTLIK LINEIEQQHF HEKSVKTINE VLEYFIKTGH VETAQTLKAI
     LFEDGLSDGI TYFENIEIPL EMVMHDLKSR TVGDCSTINV TRIPYHLDEL IRGFINYPEK
     HQILAPLFKA RVKSEADLEE AFHRLSLEMV QPEIECPISE THFERAFKKE TLDKTQAVLT
     HYFRISTGLD SKKNYQERLN DLSAYLSKES SLEKNDIKLL LSMLDSEIKP KTGVFQTLFG
     ENQNKLYKAF HKKIELQLLD SEIENKNELK