ID   APHA_AGGAD              Reviewed;         235 AA.
AC   C9R7B6;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Class B acid phosphatase {ECO:0000250|UniProtKB:P0AE22};
DE            Short=CBAP {ECO:0000250|UniProtKB:P0AE22};
DE            EC=3.1.3.2 {ECO:0000250|UniProtKB:P0AE22};
DE   Flags: Precursor;
GN   Name=aphA {ECO:0000250|UniProtKB:P0AE22}; OrderedLocusNames=D11S_0149;
OS   Aggregatibacter actinomycetemcomitans serotype C (strain D11S-1)
OS   (Actinobacillus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=668336;
RN   [1] {ECO:0000312|EMBL:ACX81568.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D11S-1 {ECO:0000269|PubMed:19820097};
RX   PubMed=19820097; DOI=10.1128/jb.01203-09;
RA   Chen C., Kittichotirat W., Si Y., Bumgarner R.;
RT   "Genome sequence of Aggregatibacter actinomycetemcomitans serotype c strain
RT   D11S-1.";
RL   J. Bacteriol. 191:7378-7379(2009).
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).
CC       {ECO:0000250|UniProtKB:P0AE22}.
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:P0AE22};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AE22};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0AE22};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AE22}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0AE22}.
CC   -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase family.
CC       {ECO:0000250|UniProtKB:P0AE22}.
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DR   EMBL; CP001733; ACX81568.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9R7B6; -.
DR   SMR; C9R7B6; -.
DR   KEGG; aat:D11S_0149; -.
DR   PATRIC; fig|668336.12.peg.144; -.
DR   OMA; PEFWEKM; -.
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   CDD; cd07499; HAD_CBAP; 1.
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   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..235
FT                   /note="Class B acid phosphatase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415224"
FT   ACT_SITE        67
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   ACT_SITE        69
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         135..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
SQ   SEQUENCE   235 AA;  26419 MW;  E10606329006CD38 CRC64;
     MKNLVKLSLI AMLTAATLPA MAAKSEPYTH QGTNAREMLV EQPIHWISVD QLKKELEGKA
     PMNISFDIDE TVLFSSPCFY HGQQKYSPGK QDYLKNQDFW NEVNAGCDQY SIPKQIAVDL
     INMHQERGDQ IYFITGRTAE DKDGVTPVLQ KAFNIKNMHP VEFMGGRDRT TKYNKTPGII
     EHKVTIHYGD SDDDILAAKE AGVRGIRLMR AANSTYQPMP TLGGYGEEVL INSSY