ID   PSTS1_MYCBP             Reviewed;         374 AA.
AC   A0A0H3M950;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Phosphate-binding protein PstS1 {ECO:0000303|PubMed:9139906};
DE            Short=PstS-1;
DE   AltName: Full=38-kDa lipoprotein;
DE            Short=P38;
DE   Flags: Precursor;
GN   Name=pstS1; OrderedLocusNames=BCG_0988;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN   [2]
RP   SUBCELLULAR LOCATION, AND INDUCTION BY PHOSPHATE STARVATION.
RC   STRAIN=BCG;
RX   PubMed=9139906; DOI=10.1128/jb.179.9.2900-2906.1997;
RA   Lefevre P., Braibant M., de Wit L., Kalai M., Roeper D., Groetzinger J.,
RA   Delville J.-P., Peirs P., Ooms J., Huygen K., Content J.;
RT   "Three different putative phosphate transport receptors are encoded by the
RT   Mycobacterium tuberculosis genome and are present at the surface of
RT   Mycobacterium bovis BCG.";
RL   J. Bacteriol. 179:2900-2906(1997).
CC   -!- FUNCTION: Functions in inorganic phosphate uptake, a phosphate-binding
CC       protein, although probably not the main uptake protein under phosphate
CC       starvation (By similarity). Part of the ABC transporter complex PstSACB
CC       involved in phosphate import (Probable). {ECO:0000250|UniProtKB:P9WGU1,
CC       ECO:0000305}.
CC   -!- FUNCTION: A host TLR2 agonist (toll-like receptor), requires both host
CC       TLR1 and TLR2 as coreceptors. {ECO:0000250|UniProtKB:P9WGU1}.
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:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Secreted {ECO:0000269|PubMed:9139906}. Note=Present on the cell
CC       surface. {ECO:0000269|PubMed:9139906}.
CC   -!- INDUCTION: By phosphate starvation (at protein level).
CC       {ECO:0000269|PubMed:9139906}.
CC   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR   EMBL; AM408590; CAL70974.1; -; Genomic_DNA.
DR   RefSeq; WP_003404786.1; NC_008769.1.
DR   AlphaFoldDB; A0A0H3M950; -.
DR   SMR; A0A0H3M950; -.
DR   KEGG; mbb:BCG_0988; -.
DR   HOGENOM; CLU_034528_1_2_11; -.
DR   OMA; NEGMSAQ; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
DR   InterPro; IPR005673; ABC_phos-bd_PstS.
DR   InterPro; IPR024370; PBP_domain.
DR   Pfam; PF12849; PBP_like_2; 1.
DR   PIRSF; PIRSF002756; PstS; 1.
DR   TIGRFAMs; TIGR00975; 3a0107s03; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Phosphate transport;
KW   Secreted; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           24..374
FT                   /note="Phosphate-binding protein PstS1"
FT                   /id="PRO_5002615734"
FT   REGION          25..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58..60
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         88
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         106
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         189..191
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   374 AA;  38215 MW;  1434968191FF201D CRC64;
     MKIRLHTLLA VLTAAPLLLA AAGCGSKPPS GSPETGAGAG TVATTPASSP VTLAETGSTL
     LYPLFNLWGP AFHERYPNVT ITAQGTGSGA GIAQAAAGTV NIGASDAYLS EGDMAAHKGL
     MNIALAISAQ QVNYNLPGVS EHLKLNGKVL AAMYQGTIKT WDDPQIAALN PGVNLPGTAV
     VPLHRSDGSG DTFLFTQYLS KQDPEGWGKS PGFGTTVDFP AVPGALGENG NGGMVTGCAE
     TPGCVAYIGI SFLDQASQRG LGEAQLGNSS GNFLLPDAQS IQAAAAGFAS KTPANQAISM
     IDGPAPDGYP IINYEYAIVN NRQKDAATAQ TLQAFLHWAI TDGNKASFLD QAHFQPLPPA
     VVKLSDALIA TISS