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Database: UniProt
Entry: Q327C8_SHIDS
LinkDB: Q327C8_SHIDS
Original site: Q327C8_SHIDS 
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
//
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