PPBH_PSEAE
ID PPBH_PSEAE Reviewed; 476 AA.
AC P35483; Q9HYU7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alkaline phosphatase H;
DE EC=3.1.3.1;
DE AltName: Full=High molecular weight phosphatase {ECO:0000303|PubMed:8454193};
DE Short=H-AP;
DE Flags: Precursor;
GN Name=phoA; OrderedLocusNames=PA3296;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 27-45, FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=H103;
RX PubMed=8454193; DOI=10.1111/j.1574-6968.1993.tb05977.x;
RA Tan A.S.P., Worobec E.A.;
RT "Isolation and characterization of two immunochemically distinct alkaline
RT phosphatases from Pseudomonas aeruginosa.";
RL FEMS Microbiol. Lett. 106:281-286(1993).
CC -!- FUNCTION: Has only phosphomonoesterase activity.
CC {ECO:0000269|PubMed:8454193}.
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:8454193}. Periplasm
CC {ECO:0000269|PubMed:8454193}.
CC -!- DEVELOPMENTAL STAGE: Expressed constitutively.
CC {ECO:0000269|PubMed:8454193}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06684.1; -; Genomic_DNA.
DR PIR; A83235; A83235.
DR RefSeq; NP_251986.1; NC_002516.2.
DR RefSeq; WP_003113164.1; NZ_QZGE01000017.1.
DR AlphaFoldDB; P35483; -.
DR SMR; P35483; -.
DR STRING; 287.DR97_4634; -.
DR PaxDb; P35483; -.
DR EnsemblBacteria; AAG06684; AAG06684; PA3296.
DR GeneID; 882459; -.
DR KEGG; pae:PA3296; -.
DR PATRIC; fig|208964.12.peg.3448; -.
DR PseudoCAP; PA3296; -.
DR HOGENOM; CLU_008539_0_1_6; -.
DR InParanoid; P35483; -.
DR OMA; CANMQVA; -.
DR PhylomeDB; P35483; -.
DR BioCyc; PAER208964:G1FZ6-3357-MON; -.
DR Proteomes; UP000002438; 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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
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 Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Periplasm;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:8454193"
FT CHAIN 27..476
FT /note="Alkaline phosphatase H"
FT /id="PRO_0000024014"
FT ACT_SITE 128
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
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 CONFLICT 27
FT /note="R -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="EY -> VR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 50409 MW; A3059B30BBEA809C CRC64;
MTPGYPLALS LAVSMAVLGS ALPAQARQDD PSLFNRQARG ELSEYGGARR VEQDLTQALK
QSLSKKKAKN VILLIGDGMG DSEITVARNY ARGAGGYFKG IDALPLTGQY THYSLHKDSG
LPDYVTDSAA SATAWSTGVK 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 SEESSQEHTG TQLRIAAYGP QAANVTGLTD QTDLFFTIRR ALNLRD
