ID   PPB_SERMA               Reviewed;         475 AA.
AC   P19147;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Alkaline phosphatase;
DE            Short=APase;
DE            EC=3.1.3.1;
DE   Flags: Precursor;
GN   Name=phoA;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2129542; DOI=10.1093/oxfordjournals.molbev.a040623;
RA   Dubose R.F., Hartl D.L.;
RT   "The molecular evolution of bacterial alkaline phosphatase: correlating
RT   variation among enteric bacteria to experimental manipulations of the
RT   protein.";
RL   Mol. Biol. Evol. 7:547-577(1990).
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.;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR   EMBL; M33965; AAA26563.1; -; Genomic_DNA.
DR   RefSeq; WP_046686693.1; NZ_WUUW01000006.1.
DR   AlphaFoldDB; P19147; -.
DR   SMR; P19147; -.
DR   STRING; 273526.SMDB11_0795; -.
DR   GeneID; 64309150; -.
DR   PATRIC; fig|615.103.peg.359; -.
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; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Magnesium; Metal-binding; Periplasm;
KW   Phosphoprotein; Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..475
FT                   /note="Alkaline phosphatase"
FT                   /id="PRO_0000024015"
FT   REGION          419..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   DISULFID        194..204
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..362
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  49265 MW;  1B8B9841CBDE6653 CRC64;
     MQPAVSLIAG AVLSALLCSS AIAAETSANA DGLTDRAARG NLVEPGGARR LAGDQTTALK
     ASLSDKTAKN VILLIGDGMG DSEITAARNY AEGAGGYFKG IDALPLTGQY THYSLDRKTH
     KPDYVTDSAA SATAWATGVK TYNGALGVDV NGKDQPTLLE IAKAAGKATG NVSTAELQDA
     TPAALVSHVI SRKCYGPEET SEKCAANALE NGGRGSITEQ LLKTRADVTL GGGAKSFNQL
     AKSGEWQGKS LKDQAAAQGY QWVSNADELQ AVTLANQQKP LLGLFADGNM PVRWLGPKAS
     YHGNLDKPAV TCENNPARTA ATPTLAAMTE KAIALLKDNP NGFFLQVEGA SIDKQDHAAN
     PCGQIGETVD LDEAVQKALA FARADGNTLV IVTADHAHAS QIVSADAKAP GLTQKLTTKD
     GAPMTLSYGN SEEESQGHTG TQLRVAAYGP HAANVVGLTD QTDLFFTMRD AMGIK