ID Q5WVJ7_LEGPL Unreviewed; 545 AA.
AC Q5WVJ7;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Alkaline phosphatase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=lpl1818 {ECO:0000313|EMBL:CAH16057.1};
OS Legionella pneumophila (strain Lens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH16057.1, ECO:0000313|Proteomes:UP000002517};
RN [1] {ECO:0000313|EMBL:CAH16057.1, ECO:0000313|Proteomes:UP000002517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens {ECO:0000313|EMBL:CAH16057.1,
RC ECO:0000313|Proteomes:UP000002517};
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH16057.1; -; Genomic_DNA.
DR RefSeq; WP_011215820.1; NC_006369.1.
DR AlphaFoldDB; Q5WVJ7; -.
DR KEGG; lpf:lpl1818; -.
DR LegioList; lpl1818; -.
DR HOGENOM; CLU_034095_0_0_6; -.
DR Proteomes; UP000002517; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:InterPro.
DR CDD; cd16016; AP-SPAP; 1.
DR Gene3D; 3.30.1360.150; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR026263; Alkaline_phosphatase_prok.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF126; PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR PIRSF; PIRSF031924; Pi-irrepressible_AP; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR031924-50};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..545
FT /note="Alkaline phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004263541"
FT ACT_SITE 74
FT /note="Phosphothreonine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031924-50"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
FT BINDING 157..159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR031924-51"
SQ SEQUENCE 545 AA; 61368 MW; A708F0F20C39A59F CRC64;
MKKISCSILL LMNSLISYAD SDQPKLILQI VVDQLRGDLI YRHHKQFGPS GFNYLLAHGL
DYHNAHHPHA NTTTCAGHST IATGSYPSLH GIVDNDWYDR KTRKLKYCME DLQAKILPTV
HTHIEISGRS PRNLKPSTLS DEIILANKGK VFGVSLKDRA AITLAGHAGK AFWFDKTNGG
FITSNYYYSS YPLWVENWNQ HYQPKAYDWN LSHPKSFYQN ANTLPFRHNY GSFGQTFPHH
VTNPPSEEYF KSLSRTPKAD ELTADFAKQL LVNEKLGKTT GQTDYLAISF SAVDAIGHQF
GPNSLEAEDN LIALDDTLSQ LFKTIDKEVG LNNTLIILTA DHGVSDGPSY LKANKIPEIK
PVNIEATGKH IEHLLLKRFN LPAQALMSIN PPFIYLDHQI IKEKNLDIAE VSFYLAEEIS
HLPGIFKAYP LPIRDIEKDW LSAKVDRMSY AYRAGDVYIV QPPYQSHGAK SEDRVAHGSP
WQYDTYVPLL FVHPDFKPKR IFRQVHTTDI APTLSSLLLI KPPAAAVGQP LVEVVNAFHK
TGEND
//
