ID   APHA_MORMO              Reviewed;         236 AA.
AC   Q59544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Class B acid phosphatase;
DE            Short=CBAP;
DE            EC=3.1.3.2 {ECO:0000269|PubMed:7894706};
DE   AltName: Full=Minor phosphate-irrepressible acid phosphatase;
DE   Flags: Precursor;
GN   Name=aphA; Synonyms=napA;
OS   Morganella morganii (Proteus morganii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-43, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RC   STRAIN=RS12;
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
CC       including 5'-AMP, 3'-AMP, pNPP, PDP, 5'-UMP, 3'-UMP, G2P, glucose 6-P
CC       and ribose 5-P. No activity toward organic phosphate diesters. Also has
CC       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. {ECO:0000269|PubMed:7894706}.
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:0000269|PubMed:7894706};
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   -!- ACTIVITY REGULATION: Activated by ethanol. Also activated by Co(2+),
CC       Zn(2+) and glycerol. Inhibited by EDTA, inorganic phosphate,
CC       nucleosides and Ca(2+). Unaffected by fluoride and tartrate.
CC       {ECO:0000269|PubMed:7894706}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 6 using pNPP as substrate. Retains more than 50%
CC         of maximal activity in the pH range 4-7.
CC         {ECO:0000269|PubMed:7894706};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7894706}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7894706}.
CC   -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; X78328; CAA55131.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59544; -.
DR   SMR; Q59544; -.
DR   STRING; 582.AL531_02900; -.
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   PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR   SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01672; AphA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Periplasm;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:7894706"
FT   CHAIN           24..236
FT                   /note="Class B acid phosphatase"
FT                   /id="PRO_0000024006"
FT   ACT_SITE        68
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   ACT_SITE        70
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         68
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         136..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
SQ   SEQUENCE   236 AA;  26683 MW;  E5F6A38D918B74D2 CRC64;
     MRKLTLTLSA LALALSLNSV ADAKVYMPEK VSDGVTVAQL AEQHAIHWIS VEQIEESLKG
     QPMAVGFDID DTVLFSSPGF YRGKLEYSPN DYSYLKNPEF WEKMNNEWDK FSMPKKSGME
     LVQMHLKRGD TVYFITGRSK TKTETVTKYV QEGLRIPADK MNPVIFAGDE EGQNNKVSWM
     RDHKLKIYYG DADADIAAAR ELNIRGIRVL RASNSSYQPL PKAGQFGEEV VINSEY