ID   PPA_ZYMMO               Reviewed;         264 AA.
AC   P14924; Q5NRA0;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=phoC; OrderedLocusNames=ZMO0130;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=2914872; DOI=10.1128/jb.171.2.767-774.1989;
RA   Pond J.L., Eddy C.K., MacKenzie K.F., Conway T., Borecky D.J., Ingram L.O.;
RT   "Cloning, sequencing, and characterization of the principal acid
RT   phosphatase, the phoC+ product, from Zymomonas mobilis.";
RL   J. Bacteriol. 171:767-774(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Most active with magnesium.;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; M24141; AAA27700.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV88754.1; -; Genomic_DNA.
DR   PIR; A32044; A32044.
DR   RefSeq; WP_011240095.1; NZ_CP035711.1.
DR   AlphaFoldDB; P14924; -.
DR   SMR; P14924; -.
DR   STRING; 264203.ZMO0130; -.
DR   GeneID; 79904625; -.
DR   KEGG; zmo:ZMO0130; -.
DR   eggNOG; COG0671; Bacteria.
DR   HOGENOM; CLU_079861_1_0_5; -.
DR   Proteomes; UP000001173; 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   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; Magnesium; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..264
FT                   /note="Acid phosphatase"
FT                   /id="PRO_0000024003"
FT   CONFLICT        17
FT                   /note="I -> V (in Ref. 1; AAA27700)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   264 AA;  29004 MW;  CAA302345B31A2BD CRC64;
     MIKVPRFICM IALTSGILAS GLSQSVSAHT EKSEPSSTYH FHSDPLLYLA PPPTSGSPLQ
     AHDDQTFNST RQLKGSTRWA LATQDADLHL ASVLKDYACA AGMNLDIAQL PHLANLIKRA
     LRTEYDDIGR AKNNWNRKRP FVDTDQPICT EKDREGLGKQ GSYPSGHTTI GWSVALILAE
     LIPDHAANIL QRGQIFGTSR IVCGAHWFSD VQAGYIMASG EIAALHGDAD FRRDMELARK
     ELEKARTSAH TPDDLLCKIE QSAR
//