PPBH_PSEAB
ID PPBH_PSEAB Reviewed; 476 AA.
AC Q02QC9;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Alkaline phosphatase H {ECO:0000255|PROSITE-ProRule:PRU10042};
DE EC=3.1.3.1 {ECO:0000255|PROSITE-ProRule:PRU10042};
DE AltName: Full=High molecular weight phosphatase;
DE Short=H-AP;
DE Flags: Precursor;
GN Name=phoA; OrderedLocusNames=PA14_21410;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-128.
RC STRAIN=UCBPP-PA14;
RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL Anal. Bioanal. Chem. 406:6297-6309(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-128 AND SER-206.
RC STRAIN=UCBPP-PA14;
RX PubMed=24965220; DOI=10.1002/pmic.201400190;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT aeruginosa PA14 strain.";
RL Proteomics 14:2017-2030(2014).
CC -!- FUNCTION: Has only phosphomonoesterase activity.
CC {ECO:0000250|UniProtKB:P35483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10042};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}. Periplasm
CC {ECO:0000250|UniProtKB:P35483}.
CC -!- MISCELLANEOUS: There are 2 known alkaline phosphatase proteins in
CC P.aeruginosa strain PAO1. The larger is well conserved in strain PA14
CC (this entry), but the other is not well conserved. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000255|RuleBase:RU003946}.
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DR EMBL; CP000438; ABJ12547.1; -; Genomic_DNA.
DR RefSeq; WP_003112133.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02QC9; -.
DR SMR; Q02QC9; -.
DR iPTMnet; Q02QC9; -.
DR PRIDE; Q02QC9; -.
DR EnsemblBacteria; ABJ12547; ABJ12547; PA14_21410.
DR KEGG; pau:PA14_21410; -.
DR HOGENOM; CLU_008539_0_1_6; -.
DR OMA; CANMQVA; -.
DR BioCyc; PAER208963:G1G74-1771-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Periplasm; Phosphoprotein; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..476
FT /note="Alkaline phosphatase H"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431467"
FT ACT_SITE 128
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042,
FT ECO:0000269|PubMed:24965220, ECO:0000269|PubMed:25096199"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24965220,
FT ECO:0000269|PubMed:25096199"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24965220"
SQ SEQUENCE 476 AA; 50393 MW; CC4D5F2BCDADE688 CRC64;
MTPGYPLALS LAVSMAVLGS ALPAQARQDD PSLFNRQARG ELSEYGGARR VEQDLTQALK
QSLSKKKAKN VILLIGDGMG DSEITVARNY ARGAGGYFKG IDALPLTGQY THYSLHKDSG
LPDYVTDSAA SATAWTTGVK SYNGAIGVDI HEQPHRNLLE LAKLNGKATG NVSTAELQDA
TPAALLAHVT ARKCYGPEAT SKQCPSNALE NGGAGSITEQ WLKTRPDVVL GGGAATFAET
AKAGRYAGKT LRAQAEARGY RIVENLDELK AVRRANQKQP LIGLFAPGNM PVRWLGPTAT
YHGNLNQPAV SCEANPKRTA DIPTLAQMTS KAIELLKDNP NGFFLQVEGA SIDKQDHAAN
PCGQIGETVD LDEAVQKALA FAKADGETLV IVTADHAHSS QIIPPETAAP GLTQLLTTKD
GAPLAISYGN SEEGSQEHTG TQLRIAAYGP QAANVTGLTD QTDLFFTIRR ALNLRD
