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 27-MAR-2024, entry version 84. 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; Pseudomonadota; 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}. 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; CP000438; ABJ12547.1; -; Genomic_DNA. DR RefSeq; WP_003112133.1; NZ_CP034244.1. DR AlphaFoldDB; Q02QC9; -. DR SMR; Q02QC9; -. DR iPTMnet; Q02QC9; -. DR KEGG; pau:PA14_21410; -. DR PseudoCAP; PA14_21410; -. DR HOGENOM; CLU_008539_0_1_6; -. DR BioCyc; PAER208963:G1G74-1771-MONOMER; -. 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; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR001952; Alkaline_phosphatase. DR InterPro; IPR018299; Alkaline_phosphatase_AS. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1. DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1. DR Pfam; PF00245; Alk_phosphatase; 2. DR PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 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 //