PSTS_PSEAB
ID PSTS_PSEAB Reviewed; 323 AA.
AC Q02DZ3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Phosphate-binding protein PstS;
DE Flags: Precursor;
GN Name=pstS; OrderedLocusNames=PA14_70860;
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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=UCBPP-PA14;
RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL Anal. Bioanal. Chem. 406:6297-6309(2014).
RN [3]
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: Involved in the system for phosphate transport across the
CC cytoplasmic membrane. The ability of PstS to bind phosphate may allow
CC it to acquire phosphate from its host. {ECO:0000250|UniProtKB:G3XDA8}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:G3XDA8}.
CC Secreted {ECO:0000269|PubMed:24372739}. Note=Forms long appendages
CC distinct from flagella or pili on the cell surface in approximately 1%
CC of cells, 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 alkaline phosphatase L (phoA2, protein DING).
CC {ECO:0000269|PubMed:24372739}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ14752.1; -; Genomic_DNA.
DR RefSeq; WP_003096673.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02DZ3; -.
DR SMR; Q02DZ3; -.
DR PRIDE; Q02DZ3; -.
DR EnsemblBacteria; ABJ14752; ABJ14752; PA14_70860.
DR KEGG; pau:PA14_70860; -.
DR HOGENOM; CLU_026228_6_0_6; -.
DR OMA; FKKKALC; -.
DR BioCyc; PAER208963:G1G74-5963-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:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR024370; PBP_domain.
DR InterPro; IPR011862; Phos-bd.
DR Pfam; PF12849; PBP_like_2; 1.
DR TIGRFAMs; TIGR02136; ptsS_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Periplasm; Phosphate transport; Secreted; Signal; Transport;
KW Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..323
FT /note="Phosphate-binding protein PstS"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431611"
SQ SEQUENCE 323 AA; 34474 MW; EEAD5F6D4E573A75 CRC64;
MKLKRLMAAL TFVAAGVGAA SAVAAIDPAL PEYQKASGVS GNLSSVGSDT LANLMTMWAE
EYKRLYPNVN IQIQAAGSST APPALTEGTA NLGPMSRKMK DVELQAFEQK YGYKPTAVPV
AVDALAIFVH KDNPIKGLTM QQVDAIFSAT RLCGSKQDVK TWGDLGLTGD WAKKPVQLFG
RNSVSGTYGY FKEEALCKGD FRPNVNEQPG SASVVQSVSQ SLNGIGYSGI GYKTASVKTV
ALAKKEGAAF VEDNEQNALN GTYPLSRFLY VYVNKAPNKP LDPLEAQFLK LVLSKTGQQV
VVKDGYIPLP AKVAEKAIKE LGL