PPB_ESCF3
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 03-AUG-2022, entry version 131.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 / JCM
RC 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}.
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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 EnsemblBacteria; CAQ90135; CAQ90135; EFER_2640.
DR KEGG; efe:EFER_2640; -.
DR HOGENOM; CLU_008539_0_1_6; -.
DR OMA; CANMQVA; -.
DR OrthoDB; 585847at2; -.
DR BioCyc; EFER585054:EFER_RS13295-MON; -.
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 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..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
