PHON_SALTI
ID PHON_SALTI Reviewed; 250 AA.
AC Q934J6;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Non-specific acid phosphatase;
DE Short=NSAP;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=phoN; OrderedLocusNames=STY4519, t4225;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rao A.S., Mukhopadhyaya R., Mahajan S.K.;
RT "phoN, a gene for acid phosphatase from Salmonella typhi.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
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).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AF366353; AAK50861.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD09303.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71687.1; -; Genomic_DNA.
DR RefSeq; NP_458615.1; NC_003198.1.
DR RefSeq; WP_001785756.1; NZ_WSUR01000022.1.
DR AlphaFoldDB; Q934J6; -.
DR SMR; Q934J6; -.
DR STRING; 220341.16505305; -.
DR EnsemblBacteria; AAO71687; AAO71687; t4225.
DR KEGG; stt:t4225; -.
DR KEGG; sty:STY4519; -.
DR PATRIC; fig|220341.7.peg.4623; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_079861_0_0_6; -.
DR OMA; TPRWELA; -.
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 CDD; cd03397; PAP2_acid_phosphatase; 1.
DR InterPro; IPR001011; Acid_Pase_classA_bac.
DR InterPro; IPR018296; Acid_Pase_classA_bac_CS.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000897; Acid_Ptase_ClsA; 1.
DR PRINTS; PR00483; BACPHPHTASE.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
DR PROSITE; PS01157; ACID_PHOSPH_CL_A; 1.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..250
FT /note="Non-specific acid phosphatase"
FT /id="PRO_0000024001"
SQ SEQUENCE 250 AA; 28459 MW; 02B92D2035F4FE82 CRC64;
MKSRYLLFFL PLIVAKYTSA ATMQPFHSPE ESVNSQFYLP PPPGNDDPAF RYDKEAYFKG
YAIKGSPRWK QAAEDADISV ENIARIFSPV VGAKINPKDT PETWNMLQNL LKMGGYYATA
SAKKYYMRTR PFVLFNHSTC RPEDENTLRK DGSYPSGHTA YSTLLALVLS QARPERAQEL
ARRGWEFGQS RVICGAHWQS DVDAGRYVGA VEFARLQTIP AFQKSLAKVR EELNDKNNLL
SKEERPELNY