ID   APHA_KLEP3              Reviewed;         237 AA.
AC   B5XXX7;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Class B acid phosphatase {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:ACI07686.1};
DE            Short=CBAP {ECO:0000250|UniProtKB:P0AE22};
DE            EC=3.1.3.2 {ECO:0000250|UniProtKB:P0AE22, ECO:0000312|EMBL:ACI07686.1};
DE   Flags: Precursor;
GN   Name=aphA {ECO:0000312|EMBL:ACI07686.1}; OrderedLocusNames=KPK_5233;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1] {ECO:0000312|EMBL:ACI07686.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342 {ECO:0000269|PubMed:18654632};
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI07686.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XXX7; -.
DR   SMR; B5XXX7; -.
DR   EnsemblBacteria; ACI07686; ACI07686; KPK_5233.
DR   KEGG; kpe:KPK_5233; -.
DR   HOGENOM; CLU_081496_0_0_6; -.
DR   OMA; PEFWEKM; -.
DR   OrthoDB; 1258380at2; -.
DR   Proteomes; UP000001734; Chromosome.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..237
FT                   /note="Class B acid phosphatase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000415227"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   ACT_SITE        71
FT                   /note="Proton donor"
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         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         137..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
SQ   SEQUENCE   237 AA;  26137 MW;  8E0A31C5A8EB5721 CRC64;
     MRKLTLAFAA ASLLFTLNSA VVARASTPQP LWVGTNVAQL AEQAPIHWVS VAQIENSLLG
     RPPMAVGFDI DDTVLFSSPG FWRGQKTFSP GSEDYLKNPQ FWEKMNNGWD EFSMPKEVAR
     QLIAMHVKRG DSIWFVTGRS QTKTETVSKT LQDDFLIPAA NMNPVIFAGD KPGQNTKTQW
     LQAKQIKVFY GDSDNDITAA REAGARGIRV LRAANSSYKP LPMAGALGEE VIVNSEY