PPBL_PSEAB
ID PPBL_PSEAB Reviewed; 392 AA.
AC Q02HI0;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
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:24372739};
DE Flags: Precursor;
GN Name=phoA2 {ECO:0000305}; Synonyms=dinG {ECO:0000303|PubMed:24372739};
GN OrderedLocusNames=PA14_55410;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
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:0000305|PubMed:24372739}. Periplasm
CC {ECO:0000250|UniProtKB:P35482}. Note=Forms long appendages distinct
CC from flagella or pili on the cell surface in approximately 1% of cells.
CC When overexpressed more cells form more appendages.
CC {ECO:0000269|PubMed:24372739}.
CC -!- INDUCTION: Suppressed by inorganic phosphate.
CC {ECO:0000269|PubMed:24372739}.
CC -!- DISRUPTION PHENOTYPE: Strains are still able to make extracellular
CC appendages that include PstS. {ECO:0000269|PubMed:24372739}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ09831.1; -; Genomic_DNA.
DR RefSeq; WP_003141140.1; NC_008463.1.
DR AlphaFoldDB; Q02HI0; -.
DR SMR; Q02HI0; -.
DR PRIDE; Q02HI0; -.
DR EnsemblBacteria; ABJ09831; ABJ09831; PA14_55410.
DR KEGG; pau:PA14_55410; -.
DR HOGENOM; CLU_047926_0_0_6; -.
DR OMA; GRITYMS; -.
DR BioCyc; PAER208963:G1G74-4667-MON; -.
DR Proteomes; UP000000653; Chromosome.
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 2: Evidence at transcript level;
KW Hydrolase; Periplasm; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..392
FT /note="Alkaline phosphatase L"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431610"
SQ SEQUENCE 392 AA; 40714 MW; 1F055BF2387A2182 CRC64;
MYKRSLIAAS LSVAALVSAQ AMADINGGGA TLPQQLYQEP GVLTAGFAAY IGVGSGNGKA
AFLNNDYTKF VAGTTNKNVH WAGSDSKLSK TNETNPYLSA HGSAWGPLIQ VPSVATSVAL
PFNKSGSNAV NFADVNTLCG VFSGRLTDWS QIPGSGRSGA ITVVYRSESS GTTELFTRFL
NASCSSTLEG GTFAITTSFG SSFSGGLPAG AVSAQGSQAV MNALNAAQGR ITYMSPDFAA
PTLAGLDDAT KVAQVRGVSP APANVSAAIG AVTPPTTAQR SDPNNWVPVF AATANPNDPS
VRPYPTSGYP ILGFTNLIFS QCYANATQTQ QVRDFFTRHY GATANNDTAI TNHRFVPLPA
SWKLAVRQSF LTSTNNLYIG HSNVCNGIGR PL