GenomeNet

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   07-NOV-2018, entry version 117.
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 / 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;
RA   Dubose R.F., Hartl D.L.;
RT   "The molecular evolution of bacterial alkaline phosphatase:
RT   correlating variation among enteric bacteria to experimental
RT   manipulations of the protein.";
RL   Mol. Biol. Evol. 7:547-577(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / 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.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   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: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate. {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.
CC       {ECO:0000305}.
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   ProteinModelPortal; P21948; -.
DR   SMR; P21948; -.
DR   PRIDE; P21948; -.
DR   EnsemblBacteria; CAQ90135; CAQ90135; EFER_2640.
DR   KEGG; efe:EFER_2640; -.
DR   HOGENOM; HOG000099117; -.
DR   KO; K01077; -.
DR   OMA; IDMAHHA; -.
DR   OrthoDB; POG091H0B8M; -.
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; IPR017849; Alkaline_Pase-like_a/b/a.
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   Complete proteome; Disulfide bond; Hydrolase; Magnesium;
KW   Metal-binding; Periplasm; Phosphoprotein; Signal; Zinc.
FT   SIGNAL        1     21
FT   CHAIN        22    472       Alkaline phosphatase.
FT                                /FTId=PRO_0000024013.
FT   ACT_SITE    125    125       Phosphoserine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10042}.
FT   METAL        74     74       Magnesium. {ECO:0000250}.
FT   METAL        74     74       Zinc 2. {ECO:0000250}.
FT   METAL       176    176       Magnesium. {ECO:0000250}.
FT   METAL       178    178       Magnesium. {ECO:0000250}.
FT   METAL       345    345       Magnesium. {ECO:0000250}.
FT   METAL       350    350       Zinc 1. {ECO:0000250}.
FT   METAL       354    354       Zinc 1. {ECO:0000250}.
FT   METAL       392    392       Zinc 2. {ECO:0000250}.
FT   METAL       393    393       Zinc 2. {ECO:0000250}.
FT   METAL       435    435       Zinc 1. {ECO:0000250}.
FT   DISULFID    191    201       {ECO:0000250}.
FT   DISULFID    309    359       {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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