ID   PHOC_MORMO              Reviewed;         249 AA.
AC   P28581;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-MAY-2023, entry version 99.
DE   RecName: Full=Major phosphate-irrepressible acid phosphatase;
DE            Short=HPAP;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=phoC;
OS   Morganella morganii (Proteus morganii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-40.
RC   STRAIN=RS12;
RX   PubMed=8081499; DOI=10.1099/00221287-140-6-1341;
RA   Thaller M.C., Berlutti F., Schippa S., Lombardi G., Rossolini G.M.;
RT   "Characterization and sequence of PhoC, the principal phosphate-
RT   irrepressible acid phosphatase of Morganella morganii.";
RL   Microbiology 140:1341-1350(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8019 / CCM 680 / DSM 30117 / NCIMB 10466;
RX   PubMed=10877772; DOI=10.1128/aem.66.7.2811-2816.2000;
RA   Mihara Y., Utagawa T., Yamada H., Asano Y.;
RT   "Phosphorylation of nucleosides by the mutated acid phosphatase from
RT   Morganella morganii.";
RL   Appl. Environ. Microbiol. 66:2811-2816(2000).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 6.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; X64444; CAA45774.1; -; Genomic_DNA.
DR   EMBL; AB035805; BAA96744.1; -; Genomic_DNA.
DR   PIR; S19187; S19187.
DR   RefSeq; WP_004235240.1; NZ_WJFN01000003.1.
DR   AlphaFoldDB; P28581; -.
DR   SMR; P28581; -.
DR   STRING; 582.AL531_08310; -.
DR   GeneID; 69678512; -.
DR   PATRIC; fig|582.25.peg.1493; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:8081499"
FT   CHAIN           21..249
FT                   /note="Major phosphate-irrepressible acid phosphatase"
FT                   /id="PRO_0000023999"
SQ   SEQUENCE   249 AA;  26999 MW;  C43F3698052B6A5C CRC64;
     MKKNIIAGCL FSLFSLSALA AIPAGNDATT KPDLYYLKNE QAIDSLKLLP PPPEVGSIQF
     LNDQAMYEKG RMLRNTERGK QAQADADLAA GGVATAFSGA FGYPITEKDS PELYKLLTNM
     IEDAGDLATR SAKEHYMRIR PFAFYGTETC NTKDQKKLST NGSYPSGHTS IGWATALVLA
     EVNPANQDAI LERGYQLGQS RVICGYHWQS DVDAARIVGS AAVATLHSDP AFQAQLAKAK
     QEFAQKSQK
//