ID Q5ZRR1_LEGPH Unreviewed; 319 AA.
AC Q5ZRR1;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN OrderedLocusNames=lpg2819 {ECO:0000313|EMBL:AAU28867.1};
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 {ECO:0000313|EMBL:AAU28867.1, ECO:0000313|Proteomes:UP000000609};
RN [1] {ECO:0000313|EMBL:AAU28867.1, ECO:0000313|Proteomes:UP000000609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC {ECO:0000313|Proteomes:UP000000609};
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] {ECO:0007829|PDB:4TVV}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 21-319, AND DISULFIDE BONDS.
RX PubMed=25339170; DOI=10.1074/jbc.M114.592568;
RA Weber S., Stirnimann C.U., Wieser M., Frey D., Meier R., Engelhardt S.,
RA Li X., Capitani G., Kammerer R.A., Hilbi H.;
RT "A type IV translocated Legionella cysteine phytase counteracts
RT intracellular growth restriction by phytate.";
RL J. Biol. Chem. 289:34175-34188(2014).
RN [3] {ECO:0007829|PDB:7SDB}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-319, AND DISULFIDE BONDS.
RA Cleland C.P., Mosimann S.C.;
RT "Structure of the PTP-like myo-inositol phosphatase from Legionella
RT pneumophila str. Paris in complex with myo-inositol hexakisphosphate.";
RL Submitted (SEP-2021) to the PDB data bank.
RN [4] {ECO:0007829|PDB:7SDD}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 21-319, AND DISULFIDE BONDS.
RA Cleland C.P., Mosimann S.C.;
RT "Structure of the PTP-like myo-inositol phosphatase from Legionella
RT pneumophila str. Paris in complex with myo-inositol-(1,3,4,5)-
RT tetrakisphosphate.";
RL Submitted (SEP-2021) to the PDB data bank.
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DR EMBL; AE017354; AAU28867.1; -; Genomic_DNA.
DR RefSeq; WP_010948506.1; NC_002942.5.
DR RefSeq; YP_096814.1; NC_002942.5.
DR PDB; 4TVV; X-ray; 1.40 A; A/B/C/D=21-319.
DR PDB; 7SDB; X-ray; 2.00 A; A=21-319.
DR PDB; 7SDD; X-ray; 1.85 A; A=21-319.
DR PDBsum; 4TVV; -.
DR AlphaFoldDB; Q5ZRR1; -.
DR SMR; Q5ZRR1; -.
DR STRING; 272624.lpg2819; -.
DR PaxDb; 272624-lpg2819; -.
DR GeneID; 66491990; -.
DR KEGG; lpn:lpg2819; -.
DR PATRIC; fig|272624.6.peg.3002; -.
DR eggNOG; COG2453; Bacteria.
DR HOGENOM; CLU_061993_2_0_6; -.
DR OrthoDB; 21920at2; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14495; PTPLP-like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR23339:SF98; CYCLIN-DEPENDENT KINASE INHIBITOR 3-RELATED; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF14566; PTPlike_phytase; 1.
DR SMART; SM01301; PTPlike_phytase; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4TVV, ECO:0007829|PDB:7SDB};
KW Reference proteome {ECO:0000313|Proteomes:UP000000609};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..319
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004265058"
FT BINDING 51
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 203
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 232
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 233
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 235
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 236
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 237
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 270
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 277
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 286
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT BINDING 289
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0007829|PDB:7SDB"
FT DISULFID 29..37
FT /evidence="ECO:0007829|PDB:4TVV, ECO:0007829|PDB:7SDB"
SQ SEQUENCE 319 AA; 36333 MW; CD339594C7C0C3E8 CRC64;
MSFKGFKVVM LILLSTQSYA SKLASSIVCD STIENPCIVQ DSKTQFSPVI RYREVASIAD
VYGGNITGIN KFHLSGSEQP SEKGWEAIAE SISRKMGAET KKVIVLDLRQ ESHGYLNGRA
ITLVSAYNWI NLGKSNSQST LDQENWLAGL RSRKIVNGVL TVPQYVAKQY SQGKSMVVST
VKNEEYYVYK KGFDYYRIFI SDHRAPLDSE VDALVALIKN NPEDTWYHVH CRGGKGRTTT
VFAMFDMLKN ADKVSFEEII ARQASIPPFY NLMVTNREIP ELTPYYEQRL QFLIHFYEFA
RQSLMGYSGT WSEWKKLNI
//
