PSTS_PSEAE
ID PSTS_PSEAE Reviewed; 323 AA.
AC G3XDA8; Q7DC39; Q9Z9M3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Phosphate-binding protein PstS;
DE Flags: Precursor;
GN Name=pstS; OrderedLocusNames=PA5369;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16232467; DOI=10.1016/s1389-1723(99)80031-0;
RA Wu H., Kosaka H., Kato J., Kuroda A., Ikeda T., Takiguchi N., Ohtake H.;
RT "Cloning and characterization of Pseudomonas putida genes encoding the
RT phosphate-specific transport system.";
RL J. Biosci. Bioeng. 87:273-279(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 25-34, AND INDUCTION BY PHOSPHATE STARVATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12596240; DOI=10.1002/jobm.200390002;
RA Madhusudhan K.T., McLaughlin R., Komori N., Matsumoto H.;
RT "Identification of a major protein upon phosphate starvation of Pseudomonas
RT aeruginosa PAO1.";
RL J. Basic Microbiol. 43:36-46(2003).
RN [4]
RP FUNCTION IN HOST CELL ADHESION, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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 [5]
RP PROTEIN SEQUENCE OF 26-39, FUNCTION IN PHOSPHATE TRANSPORT, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND PHOSPHATE-BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX DOI=10.1111/j.1574-6968.1988.tb02602.x;
RA Worobec E.A., Siehnel R.J., Gladman P., Hancock R.E.;
RT "Gene cloning and expression of the Pseudomonas aeruginosa periplasmic
RT phosphate-binding protein.";
RL FEMS Microbiol. Lett. 52:235-238(1988).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION BY PHOSPHATE
RP STARVATION, DISRUPTION PHENOTYPE, AND PHOSPHATE-BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=6436026; DOI=10.1111/j.1432-1033.1984.tb08508.x;
RA Poole K., Hancock R.E.;
RT "Phosphate transport in Pseudomonas aeruginosa. Involvement of a
RT periplasmic phosphate-binding protein.";
RL Eur. J. Biochem. 144:607-612(1984).
RN [7]
RP BIOTECHNOLOGY.
RX PubMed=16232935; DOI=10.1263/jbb.90.688;
RA Kuroda A., Kunimoto H., Morohoshi T., Ikeda T., Kato J., Takiguchi N.,
RA Miya A., Ohtake H.;
RT "Evaluation of phosphate removal from water by immobilized phosphate-
RT binding protein PstS.";
RL J. Biosci. Bioeng. 90:688-690(2000).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24023943; DOI=10.1371/journal.pone.0074444;
RA Blus-Kadosh I., Zilka A., Yerushalmi G., Banin E.;
RT "The effect of pstS and phoB on quorum sensing and swarming motility in
RT Pseudomonas aeruginosa.";
RL PLoS ONE 8:E74444-E74444(2013).
RN [9]
RP PRELIMINARY CRYSTALLIZATION.
RX PubMed=25005086; DOI=10.1107/s2053230x14010279;
RA Neznansky A., Opatowsky Y.;
RT "Expression, purification and crystallization of the phosphate-binding PstS
RT protein from Pseudomonas aeruginosa.";
RL Acta Crystallogr. F 70:906-910(2014).
CC -!- FUNCTION: Binds 1 inorganic phosphate per subunit with a KD of 0.34 uM
CC (PubMed:6436026). Required for phosphate transport (Ref.5). In strain
CC PAO1 implicated in host cell adhesion; in some virulent strains (e.g.
CC MDR25 which expresses very high levels of this protein) antibody
CC fragments against this protein decrease host cell adhesion and increase
CC transepithelial resistance of human epithelial cell monolayers. Its
CC ability to bind phosphate may allow it to acquire phosphate from its
CC host (PubMed:18282104). {ECO:0000269|PubMed:18282104,
CC ECO:0000269|PubMed:6436026}.
CC -!- ACTIVITY REGULATION: Arsenate, pyrophosphate and polyphosphates up to
CC 15 residues long inhibit phosphate binding, while organic phosphates do
CC not. {ECO:0000269|PubMed:6436026}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6436026,
CC ECO:0000269|Ref.5}. Secreted {ECO:0000269|PubMed:18282104}. Note=In
CC some strains (e.g. non-MDR PAO1 and virulent clinical strain MDR25)
CC forms long appendages distinct from flagella or pili on the cell
CC surface: cell surface expression depends on type II secretion effector
CC hxcR (PubMed:18282104). {ECO:0000269|PubMed:18282104}.
CC -!- INDUCTION: By phosphate starvation (at protein level) (PubMed:12596240,
CC PubMed:6436026). Different strains have widely differing amounts of
CC protein that can be sheared from the cell surface, in order of
CC decreasing quantities MDR25 >> MDR1 > PAO1 > MDR13 (PubMed:18282104).
CC {ECO:0000269|PubMed:12596240, ECO:0000269|PubMed:18282104,
CC ECO:0000269|PubMed:6436026}.
CC -!- DISRUPTION PHENOTYPE: Decreased phosphate transport (PubMed:6436026,
CC Ref.5). In PAO1, decreased ability to adhere to and disrupt a layer of
CC human epithelial cells (PubMed:18282104). Hyper-swarming in the
CC presence and absence of phosphate; hyper-swarming is usually seen
CC during phosphate-depleted growth. Increased induction of alkaline
CC phosphatase in the presence and absence of phosphate. Double phoB-pstS
CC deletions act like phoB deletions (PubMed:24023943).
CC {ECO:0000269|PubMed:18282104, ECO:0000269|PubMed:24023943,
CC ECO:0000269|PubMed:6436026, ECO:0000269|Ref.5}.
CC -!- BIOTECHNOLOGY: Can be used to remove inorganic phosphate from water,
CC which could be used to control growth of microorganisms.
CC {ECO:0000269|PubMed:16232935}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR EMBL; AB017492; BAA75661.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08754.1; -; Genomic_DNA.
DR PIR; G82974; G82974.
DR RefSeq; NP_254056.1; NC_002516.2.
DR RefSeq; WP_003096673.1; NZ_QZGE01000020.1.
DR PDB; 4OMB; X-ray; 1.50 A; A/B/C/D=1-323.
DR PDB; 4PQJ; X-ray; 1.86 A; A/C=25-323.
DR PDBsum; 4OMB; -.
DR PDBsum; 4PQJ; -.
DR AlphaFoldDB; G3XDA8; -.
DR SMR; G3XDA8; -.
DR STRING; 287.DR97_2740; -.
DR PaxDb; G3XDA8; -.
DR PRIDE; G3XDA8; -.
DR DNASU; 880528; -.
DR EnsemblBacteria; AAG08754; AAG08754; PA5369.
DR GeneID; 880528; -.
DR KEGG; pae:PA5369; -.
DR PATRIC; fig|208964.12.peg.5626; -.
DR PseudoCAP; PA5369; -.
DR HOGENOM; CLU_026228_6_0_6; -.
DR OMA; FKKKALC; -.
DR PhylomeDB; G3XDA8; -.
DR BioCyc; PAER208964:G1FZ6-5491-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006817; P:phosphate ion transport; IMP:UniProtKB.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
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 3D-structure; Cell adhesion; Direct protein sequencing; Periplasm;
KW Phosphate transport; Reference proteome; Secreted; Signal; Transport;
KW Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12596240"
FT CHAIN 25..323
FT /note="Phosphate-binding protein PstS"
FT /id="PRO_0000431613"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:4OMB"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:4OMB"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:4OMB"
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
