ID   APHA_PROMI              Reviewed;         160 AA.
AC   P56527;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Class B acid phosphatase;
DE            Short=CBAP;
DE            EC=3.1.3.2 {ECO:0000250|UniProtKB:Q540U1};
DE   Flags: Precursor; Fragment;
GN   Name=aphA; Synonyms=napA;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3900035; DOI=10.1128/jb.164.1.123-129.1985;
RA   Charles I.G., Keyte J.W., Shaw W.V.;
RT   "Nucleotide sequence analysis of the cat gene of Proteus mirabilis:
RT   comparison with the type I (Tn9) cat gene.";
RL   J. Bacteriol. 164:123-129(1985).
RN   [2]
RP   IDENTIFICATION, AND CONCEPTUAL TRANSLATION.
RX   PubMed=7894706; DOI=10.1099/00221287-141-1-147;
RA   Thaller M.C., Lombardi G., Berlutti F., Schippa S., Rossolini G.M.;
RT   "Cloning and characterization of the NapA acid
RT   phosphatase/phosphotransferase of Morganella morganii: identification of a
RT   new family of bacterial acid-phosphatase-encoding genes.";
RL   Microbiology 141:147-154(1995).
CC   -!- FUNCTION: Dephosphorylates several organic phosphate monoesters. Also
CC       has a phosphotransferase activity catalyzing the transfer of low-energy
CC       phosphate groups from organic phosphate monoesters to free hydroxyl
CC       groups of various organic compounds (By similarity). {ECO:0000250}.
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=3.1.3.2;
CC         Evidence={ECO:0000250|UniProtKB:Q540U1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q540U1};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q540U1};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M11587; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M11587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P56527; -.
DR   SMR; P56527; -.
DR   STRING; 584.AOUC001_12150; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR005519; Acid_phosphat_B-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR010025; HAD-SF_ppase_IIIB_AphA.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF03767; Acid_phosphat_B; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01672; AphA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Periplasm; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..>160
FT                   /note="Class B acid phosphatase"
FT                   /id="PRO_0000024007"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   ACT_SITE        71
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         137..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   NON_TER         160
SQ   SEQUENCE   160 AA;  18081 MW;  395541C45A456735 CRC64;
     MRKVTLTLSA IALALSLNGA AMAKVHMPEV VSQGVTVTEL AHQQPIKWVS VAEIEKSLEG
     QAPMAVGFDI DDTFWFSSPG FYRVKLEYSP NDFSYLKNPE FWEKMNNEWD KFSMPKQVGI
     DLVQMHLKRG DTVYFITGRT QTKTETCVTK YVQEGLNIPA