ID   APHA_ACTSZ              Reviewed;         243 AA.
AC   A6VP72;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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, ECO:0000312|EMBL:ABR74769.1};
DE   Flags: Precursor;
GN   Name=aphA {ECO:0000250|UniProtKB:P0AE22}; OrderedLocusNames=Asuc_1410;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000746; ABR74769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VP72; -.
DR   SMR; A6VP72; -.
DR   STRING; 339671.Asuc_1410; -.
DR   KEGG; asu:Asuc_1410; -.
DR   eggNOG; COG3700; Bacteria.
DR   HOGENOM; CLU_081496_0_0_6; -.
DR   OrthoDB; 2234478at2; -.
DR   Proteomes; UP000001114; 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; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01672; AphA; 1.
DR   Pfam; PF03767; Acid_phosphat_B; 1.
DR   PIRSF; PIRSF017818; Acid_Ptase_B; 1.
DR   SFLD; SFLDG01127; C1.3:_Acid_Phosphatase_Like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..243
FT                   /note="Class B acid phosphatase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000258893"
FT   ACT_SITE        68
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   ACT_SITE        70
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         68
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         136..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE22"
SQ   SEQUENCE   243 AA;  27365 MW;  32E3AAF37288EB6F CRC64;
     MSLIKSSVFM FSMLTIAVSA NAKGPKVSYD HAGITAIDHK NEAQVKWVSA ESIQKELKGK
     PPITVSFDID DTVLVSSQCF YYGKQTFSPD SLDYLHNQAY WDFVADGCDN YSIPKESAKK
     LIDMHQARGD QVIFITGRTP HRLHKAGQMD QLARILERAF HIKNMKPINY THDKPIAPYK
     YDKTRFMVEN RVSIHYGDSN DDILAAREAG IRGIRVIRSA TSTNRPLPLN GGYGEEVVED
     SSY
//