ID Q327J0_SHIDS Unreviewed; 246 AA.
AC Q327J0;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN Name=phoN2/apy {ECO:0000313|EMBL:ABB64518.1};
GN OrderedLocusNames=SDY_P004 {ECO:0000313|EMBL:ABB64518.1};
OS Shigella dysenteriae serotype 1 (strain Sd197).
OG Plasmid pSD1_197 {ECO:0000313|EMBL:ABB64518.1,
OG ECO:0000313|Proteomes:UP000002716}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB64518.1, ECO:0000313|Proteomes:UP000002716};
RN [1] {ECO:0000313|EMBL:ABB64518.1, ECO:0000313|Proteomes:UP000002716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB64518.1,
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|PIRNR:PIRNR000897};
CC -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC {ECO:0000256|PIRNR:PIRNR000897}.
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DR EMBL; CP000035; ABB64518.1; -; Genomic_DNA.
DR RefSeq; WP_000850660.1; NC_007607.1.
DR RefSeq; YP_406006.1; NC_007607.1.
DR AlphaFoldDB; Q327J0; -.
DR EnsemblBacteria; ABB64518; ABB64518; SDY_P004.
DR KEGG; sdy:SDY_P004; -.
DR PATRIC; fig|300267.13.peg.5530; -.
DR HOGENOM; CLU_079861_0_0_6; -.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW Plasmid {ECO:0000313|EMBL:ABB64518.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002716};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..246
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004220916"
FT DOMAIN 106..218
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 246 AA; 27574 MW; DA1F901BEEB075F4 CRC64;
MKTKNFLLFC IATNMIFIPS ANALKAEGFL TQQTSPDSLS ILPPPPAEDS VVFQADKAHY
EFGRSLRDAN RVRLASEDAY YENFGLAFSD AYGMDISREN TPILYQLLTQ VLQDSHDYAV
RNAKEYYKRV RPFVIYKDAT CTPDKDEKMA ITGSYPSGHA SFGWAVALIL AEINPQRKAE
ILRRGYEFGE SRVICGAHWQ SDVEAGRLMG ASVVAVLHNT PEFTKSLSEA KKEFEELNTP
TNELTP
//
