PSTS2_STRPN
ID PSTS2_STRPN Reviewed; 291 AA.
AC P0C2M5; Q7D480; Q9X4T0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Phosphate-binding protein PstS 2;
DE Short=PBP 2;
DE Flags: Precursor;
GN Name=pstS2; OrderedLocusNames=SP_2084;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=WU2 / Serotype 3;
RX PubMed=11705934; DOI=10.1128/iai.69.12.7565-7571.2001;
RA Orihuela C.J., Mills J., Robb C.W., Wilson C.J., Watson D.A., Niesel D.W.;
RT "Streptococcus pneumoniae PstS production is phosphate responsive and
RT enhanced during growth in the murine peritoneal cavity.";
RL Infect. Immun. 69:7565-7571(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [3]
RP ROLE IN PENICILLIN RESISTANCE.
RX PubMed=16313627; DOI=10.1111/j.1365-2958.2005.04914.x;
RA Soualhine H., Brochu V., Menard F., Papadopoulou B., Weiss K.,
RA Bergeron M.G., Legare D., Drummelsmith J., Ouellette M.;
RT "A proteomic analysis of penicillin resistance in Streptococcus pneumoniae
RT reveals a novel role for PstS, a subunit of the phosphate ABC
RT transporter.";
RL Mol. Microbiol. 58:1430-1440(2005).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import. {ECO:0000305|PubMed:16313627}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PstB),
CC two transmembrane proteins (PstC and PstA) and a solute-binding protein
CC (PstS). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By phosphate starvation. {ECO:0000305|PubMed:11705934}.
CC -!- MISCELLANEOUS: Overexpression seems to confer resistance to penicillin.
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; AY039745; AAK72111.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK76144.1; -; Genomic_DNA.
DR PIR; G95243; G95243.
DR RefSeq; WP_000669493.1; NZ_AKVY01000001.1.
DR PDB; 4H1X; X-ray; 1.77 A; A=28-291.
DR PDBsum; 4H1X; -.
DR AlphaFoldDB; P0C2M5; -.
DR SMR; P0C2M5; -.
DR STRING; 170187.SP_2084; -.
DR DNASU; 931962; -.
DR EnsemblBacteria; AAK76144; AAK76144; SP_2084.
DR GeneID; 60233667; -.
DR GeneID; 66807164; -.
DR KEGG; spn:SP_2084; -.
DR eggNOG; COG0226; Bacteria.
DR OMA; GTCDIGM; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR024370; PBP_domain.
DR Pfam; PF12849; PBP_like_2; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphate transport; Signal; Stress response; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..291
FT /note="Phosphate-binding protein PstS 2"
FT /id="PRO_0000281671"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:4H1X"
FT STRAND 249..262
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:4H1X"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:4H1X"
SQ SEQUENCE 291 AA; 30757 MW; 4F534005A7DDE616 CRC64;
MKFKKMLTLA AIGLSGFGLV ACGNQSAASK QSASGTIEVI SRENGSGTRG AFTEITGILK
KDGDKKIDNT AKTAVIQNST EGVLSAVQGN ANAIGYISLG SLTKSVKALE IDGVKASRDT
VLDGEYPLQR PFNIVWSSNL SKLGQDFISF IHSKQGQQVV TDNKFIEAKT ETTEYTSQHL
SGKLSVVGST SVSSLMEKLA EAYKKENPEV TIDITSNGSS AGITAVKEKT ADIGMVSREL
TPEEGKSLTH DAIALDGIAV VVNNDNKASQ VSMAELADVF SGKLTTWDKI K
