ID   PPB_LYSEN               Reviewed;         539 AA.
AC   Q05205;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-MAY-2023, entry version 74.
DE   RecName: Full=Alkaline phosphatase;
DE            Short=APASE;
DE            EC=3.1.3.1;
DE   Flags: Precursor;
GN   Name=phoA;
OS   Lysobacter enzymogenes.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=69;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 149-179; 267-277
RP   AND 341-361.
RC   STRAIN=ATCC 29487 / DSM 2043 / BCRC 11654 / KCTC 12131 / LMG 8762 /
RC   VKM B-2235 / UASM 495 / Ly e1;
RX   PubMed=1856159; DOI=10.1128/jb.173.15.4551-4557.1991;
RA   Au S., Roy K.L., von Tigerstrom R.G.;
RT   "Nucleotide sequence and characterization of the gene for secreted alkaline
RT   phosphatase from Lysobacter enzymogenes.";
RL   J. Bacteriol. 173:4551-4557(1991).
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=3.1.3.1;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The C-terminal Pro-sequence may be required for translocation of
CC       the phosphatase across the outer membrane.
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DR   EMBL; X56656; CAA39978.1; -; Genomic_DNA.
DR   PIR; A42467; A42467.
DR   AlphaFoldDB; Q05205; -.
DR   SMR; Q05205; -.
DR   STRING; 69.GLE_5070; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR039331; PPA-like.
DR   PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR   PANTHER; PTHR22953:SF153; PURPLE ACID PHOSPHATASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..148
FT                   /evidence="ECO:0000269|PubMed:1856159"
FT                   /id="PRO_0000023994"
FT   CHAIN           149..429
FT                   /note="Alkaline phosphatase"
FT                   /id="PRO_0000023995"
FT   PROPEP          430..539
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000023996"
SQ   SEQUENCE   539 AA;  56490 MW;  C51DC38429936C3E CRC64;
     MNLSPSRTPI CAALAAALLG AAALAPAHAA QRILQLSEDT THSKPVSAAS ALRGTPLAKA
     GAADRVCEAG AKWLRVGFKQ LKLAGYDSLV LTSSGGDKLV FEGQHWNQRS FTTRPLRGEC
     VDIQPYFSQP DSAFQLDRYD YSTVALDKAT VVVAGAGDIC DTSGNACQGT SDLIVSINPT
     AVFTAGDNAY NSGTLSEYNS RYAPTWGRFK ALTSPSPGNH DYSTTGAKGY FDYFNGSGNQ
     TGPAGDRSKG YYSWDVGDWH FVSLNTMSGG TVAQAQIDWL KADLAANTKP CTAAYFHHPL
     LSRGSYSGYS QVKPFWDALY AAKADLVLVG HDHNYQRYGK MNPDKAAASD GIRQVLVGTG
     GRAFYGISGS HALLEASNDS TFGVLKLTLS ATGYTGDFVP RAGSSYTDHF TGTCNKGSGN
     PPTQTLTLNS VRDVTVKSGG SRDNGATLYA DGSDGGQVLR GLMAWNVSSA AGKTLTGAQV
     KLQVSDRSTG TYDLYRAGAA WTEANASYSG VSLGSKIGSV VPSATGAQSI ALNAAGFSW
//