ID Q327C8_SHIDS Unreviewed; 249 AA.
AC Q327C8;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 28-JUN-2023, entry version 94.
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=phoN1 {ECO:0000313|EMBL:ABB64580.1};
GN OrderedLocusNames=SDY_P067 {ECO:0000313|EMBL:ABB64580.1};
OS Shigella dysenteriae serotype 1 (strain Sd197).
OG Plasmid pSD1_197 {ECO:0000313|EMBL:ABB64580.1,
OG ECO:0000313|Proteomes:UP000002716}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB64580.1, ECO:0000313|Proteomes:UP000002716};
RN [1] {ECO:0000313|EMBL:ABB64580.1, ECO:0000313|Proteomes:UP000002716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB64580.1,
RC ECO:0000313|Proteomes:UP000002716};
RC PLASMID=Plasmid pSD1_197 {ECO:0000313|Proteomes:UP000002716};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000035; ABB64580.1; -; Genomic_DNA.
DR RefSeq; WP_000828660.1; NC_007607.1.
DR RefSeq; YP_406068.1; NC_007607.1.
DR AlphaFoldDB; Q327C8; -.
DR EnsemblBacteria; ABB64580; ABB64580; SDY_P067.
DR KEGG; sdy:SDY_P067; -.
DR PATRIC; fig|300267.13.peg.5614; -.
DR HOGENOM; CLU_079861_0_0_6; -.
DR OMA; TPRWELA; -.
DR Proteomes; UP000002716; Plasmid pSD1_197.
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:ABB64580.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002716};
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_5004220922"
FT DOMAIN 115..227
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 249 AA; 27169 MW; 604FCE0C72FC1277 CRC64;
MKRQLFTLSI VGVFSLNTFA SFPPGNDVTT KPDLYYLTND NAIDSLALLP PPPQIGSIAF
LNDQAMYEKG LLLRNTERGK LAAEDANLSS GGVANVFSAA FGSPITAKDS PELHKLLTNM
IEDAGDLATR SAKEYYMRIR PFAFYGVSTC NTKEQDTLSR NGSYPSGHTS IGWATALVLS
EINPARQDTI LKRGYELGDS RVICGYHWQS DVDAARIVGS AIVATLHSNP VFQAQLQKAK
DEFANNQKK
//