ID PPB_ESCF3 Reviewed; 472 AA. AC P21948; B7LMK2; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 02-SEP-2026, entry version 146. DE RecName: Full=Alkaline phosphatase; DE Short=APase; DE EC=3.1.3.1; DE Flags: Precursor; GN Name=phoA; OrderedLocusNames=EFER_2640; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054; 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). 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}. 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; M33966; AAA24371.1; -; Genomic_DNA. DR EMBL; CU928158; CAQ90135.1; -; Genomic_DNA. DR PIR; I57445; I57445. DR RefSeq; WP_000813782.1; NC_011740.1. DR AlphaFoldDB; P21948; -. DR SMR; P21948; -. DR GeneID; 75056330; -. DR KEGG; efe:EFER_2640; -. DR HOGENOM; CLU_008539_0_1_6; -. DR OrthoDB; 9794455at2; -. DR Proteomes; UP000000745; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd16012; ALP; 1. DR FunFam; 3.40.720.10:FF:000040; Alkaline phosphatase; 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 NCBIfam; NF007810; PRK10518.1; 1. DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1. DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1. DR Pfam; PF00245; Alk_phosphatase; 1. DR PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. PE 3: Inferred from homology; KW Disulfide bond; Hydrolase; Magnesium; Metal-binding; Periplasm; KW Phosphoprotein; Reference proteome; Signal; Zinc. FT SIGNAL 1..21 FT CHAIN 22..472 FT /note="Alkaline phosphatase" FT /id="PRO_0000024013" FT ACT_SITE 125 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042" FT BINDING 74 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 74 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 345 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 350 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 354 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 392 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 393 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 435 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT DISULFID 191..201 FT /evidence="ECO:0000250" FT DISULFID 309..359 FT /evidence="ECO:0000250" SQ SEQUENCE 472 AA; 49430 MW; EF956C964F931141 CRC64; MKQSAIALAL LSCLITPVSQ AQTSQNINIL ENRAAQGDIT MPGGARRLSG DQTEALRASL NDKPAKNIIL LIGDGMGDSE ITAARNYAEG AGGYFKGIDA LPLTGQYTHY ALDKKTGKPD YVTDSAASAT AWTTGVKTYN GALGVDIHEN PHTTILEMAK AAGLATGNVS TAELQDATPA ALVSHVTSRK CYGPSVTSEK CPGNALEKGG KGSITEQLLN ARADVTLGGG AKTFAETATA GEWQGKTLRE QALARGYQIV SDAASLAAVT QAGQDKPLLG LFAEGNMPVR WHGPKASYHG NLDKPAVTCT PNPQRNETVP TLAQMTDKAI ELLSKNERGF FLQVEGASID KQDHAANPCG QIGETVDLDE AVQRALEFAK KDGNTLVIVT ADHAHSSQIV APDTKAPGLT QALNTKDGAV MAISYGNSEE DSQEHTGSQL RIAAYGPNAA NVVGLTDQTD LFYTMKAALG LQ //