PSTS_BORBU
ID PSTS_BORBU Reviewed; 279 AA.
AC O51233;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphate-binding protein PstS {ECO:0000303|PubMed:24318969};
DE Short=PBP;
DE Flags: Precursor;
GN Name=pstS {ECO:0000303|PubMed:24318969};
GN OrderedLocusNames=BB_0215 {ECO:0000312|EMBL:AAC66609.2};
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326 {ECO:0000312|EMBL:AAC66609.2};
RN [1] {ECO:0000312|EMBL:AAC66609.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31
RC {ECO:0000312|Proteomes:UP000001807};
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2] {ECO:0007744|PDB:4N13}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 20-279, FUNCTION,
RP PHOSPHATE-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31
RC {ECO:0000303|PubMed:24318969};
RX PubMed=24318969; DOI=10.1002/pro.2406;
RA Brautigam C.A., Ouyang Z., Deka R.K., Norgard M.V.;
RT "Sequence, biophysical, and structural analyses of the PstS lipoprotein
RT (BB0215) from Borrelia burgdorferi reveal a likely binding component of an
RT ABC-type phosphate transporter.";
RL Protein Sci. 23:200-212(2014).
CC -!- FUNCTION: Binds inorganic phosphate with a Kd of 1.2 uM
CC (PubMed:24318969). Part of the ABC transporter complex PstSACB involved
CC in phosphate import (Probable). {ECO:0000269|PubMed:24318969,
CC ECO:0000305}.
CC -!- SUBUNIT: Monomer (in vitro) (PubMed:24318969). The complex is composed
CC of two ATP-binding proteins (PstB), two transmembrane proteins (PstC
CC and PstA) and a solute-binding protein (PstS) (Probable).
CC {ECO:0000269|PubMed:24318969, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24318969};
CC Lipid-anchor {ECO:0000305|PubMed:24318969}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR EMBL; AE000783; AAC66609.2; -; Genomic_DNA.
DR RefSeq; NP_212349.2; NC_001318.1.
DR RefSeq; WP_002556814.1; NC_001318.1.
DR PDB; 4N13; X-ray; 1.30 A; A=20-279.
DR PDBsum; 4N13; -.
DR AlphaFoldDB; O51233; -.
DR SMR; O51233; -.
DR STRING; 224326.BB_0215; -.
DR TCDB; 3.A.1.7.5; the atp-binding cassette (abc) superfamily.
DR PRIDE; O51233; -.
DR EnsemblBacteria; AAC66609; AAC66609; BB_0215.
DR KEGG; bbu:BB_0215; -.
DR PATRIC; fig|224326.49.peg.612; -.
DR HOGENOM; CLU_026228_5_1_12; -.
DR OMA; FKKKALC; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IGC:UniProtKB.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IGC:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB.
DR InterPro; IPR024370; PBP_domain.
DR Pfam; PF12849; PBP_like_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphate transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..279
FT /note="Phosphate-binding protein PstS"
FT /id="PRO_0000436554"
FT BINDING 33..35
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT BINDING 63
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT BINDING 151..153
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 94..107
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4N13"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:4N13"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4N13"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4N13"
SQ SEQUENCE 279 AA; 31118 MW; 9003D18BF0511D0C CRC64;
MKKVIILIFM LSTSLLYNCK NQDNEKIVSI GGSTTVSPIL DEMILRYNKI NNNTKVTYDA
QGSSVGINGL FNKIYKIAIS SRDLTKEEIE QGAKETVFAY DALIFITSPE IKITNITEEN
LAKILNGEIQ NWKQVGGPDA KINFINRDSS SGSYSSIKDL LLNKIFKTHE EAQFRQDGIV
VKSNGEVIEK TSLTPHSIGY IGLGYAKNSI EKGLNILSVN STYPTKETIN SNKYTIKRNL
IIVTNNKYED KSVTQFIDFM TSSTGQDIVE EQGFLGIKT
