ID   APHA_SALTI              Reviewed;         237 AA.
AC   O08430;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Class B acid phosphatase;
DE            Short=CBAP;
DE            EC=3.1.3.2 {ECO:0000269|PubMed:25848029};
DE   Flags: Precursor;
GN   Name=aphA; Synonyms=napA; OrderedLocusNames=STY4445, t4155;
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=STY4;
RX   PubMed=10564784; DOI=10.1111/j.1574-6968.1999.tb08821.x;
RA   Rossolini G.M., Bonci A., Schippa S., Berlutti F., Thaller M.C.;
RT   "Genetic rearrangements in the tyrB-uvrA region of the enterobacterial
RT   chromosome: a potential cause for different class B acid phosphatase
RT   regulation in Salmonella enterica and Escherichia coli.";
RL   FEMS Microbiol. Lett. 181:17-23(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX   PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA   Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA   Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA   Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA   Allen K.N., Farelli J.D.;
RT   "Panoramic view of a superfamily of phosphatases through substrate
RT   profiling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
CC   -!- FUNCTION: Dephosphorylates several organic phosphate monoesters
CC       including monophosphate nucleotides (NMPs), coenzyme A (CoA),
CC       nicotinamide adenine dinucleotide phosphate (NADP), flavin
CC       mononucleotide (FMN) and phosphorylated 5-6 carbon sugars in vitro
CC       (PubMed:25848029). Also has a phosphotransferase activity catalyzing
CC       the transfer of low-energy phosphate groups from organic phosphate
CC       monoesters to free hydroxyl groups of various organic compounds (By
CC       similarity). {ECO:0000250|UniProtKB:P58683,
CC       ECO:0000269|PubMed:25848029}.
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:25848029};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25848029};
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}.
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DR   EMBL; AJ237788; CAB40974.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD09233.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71619.1; -; Genomic_DNA.
DR   RefSeq; NP_458547.1; NC_003198.1.
DR   RefSeq; WP_000724436.1; NZ_WSUR01000027.1.
DR   AlphaFoldDB; O08430; -.
DR   SMR; O08430; -.
DR   STRING; 220341.gene:17588277; -.
DR   KEGG; stt:t4155; -.
DR   KEGG; sty:STY4445; -.
DR   PATRIC; fig|220341.7.peg.4546; -.
DR   eggNOG; COG3700; Bacteria.
DR   HOGENOM; CLU_081496_0_0_6; -.
DR   OMA; PEFWEKM; -.
DR   OrthoDB; 2234478at2; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Metal-binding; Periplasm; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..237
FT                   /note="Class B acid phosphatase"
FT                   /id="PRO_0000024008"
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   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q540U1"
FT   CONFLICT        7
FT                   /note="Missing (in Ref. 1; CAB40974)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   237 AA;  26243 MW;  3B0D71DFE7A16269 CRC64;
     MKKITLALSA VCLLFTLNHS ANALVSSPST LNPGTNVAKL AEQAPVHWVS VAQIENSLTG
     RPPMAVGFDI DDTVLFSSPG FWRGKKTYSP DSDDYLKNPA FWEKMNNGWD EFSIPKEVAR
     QLIDMHVRRG DSIYFVTGRS QTKTETVSKT LADNFHIPAA NMNPVIFAGD KPGQNTKVQW
     LQEKNMRIFY GDSDNDITAA RDCGIRGIRI LRAANSTYKP LPQAGAFGEE VIVNSEY
//