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Database: UniProt/SWISS-PROT
Entry: PPB_ESCF3
LinkDB: PPB_ESCF3
Original site: 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   24-JAN-2024, entry version 136.
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; Pseudomonadota; 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   GeneID; 75056330; -.
DR   KEGG; efe:EFER_2640; -.
DR   HOGENOM; CLU_008539_0_1_6; -.
DR   OMA; SYHGNID; -.
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   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; 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; 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
//
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