ID   PPBL_PSEAI              Reviewed;         392 AA.
AC   K4LAH1; B0YMX4;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 2.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Alkaline phosphatase L;
DE            Short=L-AP;
DE            EC=3.1.3.1 {ECO:0000250|UniProtKB:P35482};
DE   AltName: Full=Low molecular weight phosphatase;
DE   AltName: Full=Protein DING {ECO:0000303|PubMed:18282104};
DE   Flags: Precursor;
GN   Name=phoA2 {ECO:0000305}; Synonyms=dinG {ECO:0000303|PubMed:18282104};
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-42, AND
RP   INDUCTION.
RC   STRAIN=MDR1, and MDR25;
RX   PubMed=18282104; DOI=10.1371/journal.ppat.0040043;
RA   Zaborina O., Holbrook C., Chen Y., Long J., Zaborin A., Morozova I.,
RA   Fernandez H., Wang Y., Turner J.R., Alverdy J.C.;
RT   "Structure-function aspects of PstS in multi-drug-resistant Pseudomonas
RT   aeruginosa.";
RL   PLoS Pathog. 4:E43-E43(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=MDR25;
RX   PubMed=24372739; DOI=10.1111/1574-6968.12368;
RA   Shah M., Zaborin A., Alverdy J.C., Scott K., Zaborina O.;
RT   "Localization of DING proteins on PstS-containing outer-surface appendages
RT   of Pseudomonas aeruginosa.";
RL   FEMS Microbiol. Lett. 352:54-61(2014).
CC   -!- FUNCTION: Has both a phosphomonoesterase and phosphodiesterase
CC       activity. {ECO:0000250|UniProtKB:P35482}.
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         Evidence={ECO:0000250|UniProtKB:P35482};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35482}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24372739}. Periplasm
CC       {ECO:0000250|UniProtKB:P35482}. Note=In strain MDR25 forms long
CC       appendages distinct from flagella or pili on the cell surface.
CC       {ECO:0000269|PubMed:24372739}.
CC   -!- INDUCTION: Strongly induced by phosphate limitation (150-fold for MDR25
CC       smooth colonies, 1400-fold for MDR25 rough colonies and 5000-fold for
CC       MDR1) (PubMed:18282104). Highly expressed compared to the same gene in
CC       PA14, suppressed by inorganic phosphate, but less sensitive to
CC       phosphate than strain PA14. {ECO:0000269|PubMed:18282104,
CC       ECO:0000269|PubMed:24372739}.
CC   -!- MISCELLANEOUS: Protein and DNA sequence from strain MDR1 in
CC       (PubMed:18282104). DNA sequence from MDR25 in (PubMed:24372739).
CC       {ECO:0000269|PubMed:18282104, ECO:0000269|PubMed:24372739}.
CC   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR   EMBL; EF616488; ABU39826.1; -; Genomic_DNA.
DR   EMBL; JX500097; AFV08643.1; -; Genomic_DNA.
DR   RefSeq; WP_034027919.1; NZ_RWXM01000076.1.
DR   AlphaFoldDB; K4LAH1; -.
DR   SMR; K4LAH1; -.
DR   PRIDE; K4LAH1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR024370; PBP_domain.
DR   Pfam; PF12849; PBP_like_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:18282104"
FT   CHAIN           24..392
FT                   /note="Alkaline phosphatase L"
FT                   /id="PRO_0000431609"
FT   VARIANT         53
FT                   /note="A -> V (in strain: MDR25)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         164
FT                   /note="A -> V (in strain: MDR25)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         201
FT                   /note="N -> S (in strain: MDR25)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  40663 MW;  D3CF9DD75F7FB326 CRC64;
     MYKRSLIAAS LSVAALVSAQ AMAEINGGGA TLPQQLYQEP GVLTAGFAAY IGAGSGNGKA
     AFLNNDYTKF VAGTTNKNVH WAGSDSKLSK TNETNPYLSA HGSAWGPLIQ VPSVATSVAL
     PFNKSGSNAV NFADVNTLCG VFSGRLTDWS QIPGSGRSGA ITVAYRSESS GTTELFTRFL
     NASCSSALEG GTFAITTSFG NSFSGGLPAG AVSAQGSQAV MNTLNAAEGR ITYMSPDFAA
     PTLAGLDDAT KVAQVRGVSP APANVSAAIG AVTPPTTAQR SDPNNWVPVF AATASATDPS
     VRPYPTTGYP ILGFTNLIFS QCYADATQTQ QVRDFFTRHY GASVNNDTAI TNHRFVPLPA
     SWKLAVRQSF LTSTNNLYIG HSNVCNGIGR PL