APHA_SALTI
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 03-AUG-2022, entry version 135.
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; Proteobacteria; 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; 220341.16505237; -.
DR EnsemblBacteria; AAO71619; AAO71619; t4155.
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 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; -; 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 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
