ID   O50542_SHIFL            Unreviewed;       249 AA.
AC   O50542;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   03-MAY-2023, entry version 82.
DE   RecName: Full=Acid phosphatase {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000897};
DE            EC=3.1.3.2 {ECO:0000256|ARBA:ARBA00012646, ECO:0000256|PIRNR:PIRNR000897};
GN   Name=phoN {ECO:0000313|EMBL:BAA11655.1};
OS   Shigella flexneri.
OG   Plasmid pMYSH6000 {ECO:0000313|EMBL:BAA11655.1}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623 {ECO:0000313|EMBL:BAA11655.1};
RN   [1] {ECO:0000313|EMBL:BAA11655.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YSH6000 {ECO:0000313|EMBL:BAA11655.1};
RC   PLASMID=pMYSH6000 {ECO:0000313|EMBL:BAA11655.1};
RX   PubMed=8755883;
RA   Uchiya K., Tohsuji M., Nikai T., Sugihara H., Sasakawa C.;
RT   "Identification and characterization of phoN-Sf, a gene on the large
RT   plasmid of Shigella flexneri 2a encoding a nonspecific phosphatase.";
RL   J. Bacteriol. 178:4548-4554(1996).
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:0000256|ARBA:ARBA00000032,
CC         ECO:0000256|PIRNR:PIRNR000897};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00009017, ECO:0000256|PIRNR:PIRNR000897}.
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DR   EMBL; D82966; BAA11655.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50542; -.
DR   SMR; O50542; -.
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   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 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; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   PROSITE; PS01157; ACID_PHOSPH_CL_A; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Plasmid {ECO:0000313|EMBL:BAA11655.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..249
FT                   /note="Acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004158682"
FT   DOMAIN          115..227
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   249 AA;  27178 MW;  58F34CEB034EE070 CRC64;
     MKRQLFTLSI VGVFSLNTFA SIPPGNDVTT KPDLYYLTND NAIDSLALLP PPPQIGSIAF
     LNDQAMYEKG RLLRNTERGK LAAEDANLSS GGVANVFSAA FGSPITAKDS PELHKLLTNM
     IEDAGDLATR SAKEYYMRIR PFAFYGVSTC NTKEQDTLSR NGSYPSGHTS IGWATALVLS
     EINPARQDTI LKRGYELGDS RVICGYHWQS DVDAARIVGS AIVATLHSNP VFQAQLQKAK
     DEFANNQKK
//