ID   PSTS_PSEAI              Reviewed;         323 AA.
AC   P0DMR4; Q7DC39; Q9Z9M3;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Phosphate-binding protein PstS;
DE   Flags: Precursor;
GN   Name=pstS;
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 25-35, FUNCTION IN
RP   VIRULENCE, FUNCTION IN HOST CELL ADHESION, SUBCELLULAR LOCATION, AND
RP   INDUCTION BY PHOSPHATE STARVATION.
RC   STRAIN=MDR1, MDR13, 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   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: Binds 1 inorganic phosphate per subunit, required for
CC       phosphate transport (By similarity). In virulent strain MDR25, which
CC       expresses very high levels of this protein, implicated in host cell
CC       adhesion; antibody fragments against this protein decrease adhesion to
CC       host cells and increase transepithelial resistance of human epithelial
CC       cell monolayers. High-phosphate-grown MDR25 strains form smooth
CC       colonies, express less PstS, more biofilm and are less lethal in mouse
CC       infection models than high-phosphate-grown rough colonies that express
CC       more PstS, less biofilm and are more lethal in mouse infection models;
CC       whether this is phenotype is due to PstS is unknown, however feeding
CC       mice with phosphate supplements protects them from lethality. The
CC       ability of PstS to bind phosphate may allow it to acquire phosphate
CC       from its host (PubMed:18282104). {ECO:0000250|UniProtKB:G3XDA8,
CC       ECO:0000269|PubMed:18282104}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:G3XDA8}.
CC       Secreted {ECO:0000269|PubMed:18282104, ECO:0000269|PubMed:24372739}.
CC       Note=In some strains (e.g. virulent clinical strain MDR25) forms long
CC       appendages distinct from flagella or pili on the cell surface: the
CC       protein is removed from the cell surface by vigorous vortexing (2
CC       minutes) giving a cell surface sheared protein fraction.
CC       {ECO:0000269|PubMed:18282104, ECO:0000269|PubMed:24372739}.
CC   -!- INDUCTION: By phosphate starvation (at protein level), shown for
CC       protein in MDR25 and for RNA in MDR1. Different strains have widely
CC       differing amounts of protein that can be sheared from the cell surface,
CC       in order of decreasing quantities MDR25 >> MDR1 > PAO1 > MDR13
CC       (PubMed:18282104). {ECO:0000269|PubMed:18282104,
CC       ECO:0000269|PubMed:24372739}.
CC   -!- MISCELLANEOUS: Protein sequence obtained for strain MDR1, using protein
CC       removed from the cell surface by vigorous vortexing (2 minutes) on
CC       cells grown in about 300 uM phosphate. {ECO:0000269|PubMed:18282104}.
CC   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF601157; ABU93256.1; -; Genomic_DNA.
DR   EMBL; EF601158; ABU93257.1; -; Genomic_DNA.
DR   EMBL; EF601159; ABU93258.1; -; Genomic_DNA.
DR   PIR; G82974; G82974.
DR   RefSeq; WP_003096673.1; NZ_WXZX01000005.1.
DR   AlphaFoldDB; P0DMR4; -.
DR   SMR; P0DMR4; -.
DR   eggNOG; COG0226; Bacteria.
DR   OMA; FKKKALC; -.
DR   OrthoDB; 1222928at2; -.
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; Direct protein sequencing; Periplasm; Phosphate transport;
KW   Secreted; Signal; Transport; Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:18282104"
FT   CHAIN           25..323
FT                   /note="Phosphate-binding protein PstS"
FT                   /id="PRO_0000431612"
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