ID   PSTS2_MYCBP             Reviewed;         370 AA.
AC   A0A0H3MBL5;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Phosphate-binding protein PstS2 {ECO:0000303|PubMed:9139906};
DE            Short=PstS-2;
DE   AltName: Full=38-kDa lipoprotein;
DE            Short=P38;
DE   Flags: Precursor;
GN   Name=pstS2; OrderedLocusNames=BCG_0985c;
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:P9WGT9,
CC       ECO:0000305}.
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; CAL70971.1; -; Genomic_DNA.
DR   RefSeq; WP_003404784.1; NC_008769.1.
DR   AlphaFoldDB; A0A0H3MBL5; -.
DR   SMR; A0A0H3MBL5; -.
DR   GeneID; 45424898; -.
DR   KEGG; mbb:BCG_0985c; -.
DR   HOGENOM; CLU_034528_0_0_11; -.
DR   OMA; QFVYAYI; -.
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..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..370
FT                   /note="Phosphate-binding protein PstS2"
FT                   /id="PRO_5002615602"
FT   BINDING         54..56
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         84
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         102
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         191..193
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   370 AA;  37848 MW;  36151162549B3B58 CRC64;
     MKFARSGAAV SLLAAGTLVL TACGGGTNSS SSGAGGTSGS VHCGGKKELH SSGSTAQENA
     MEQFVYAYVR SCPGYTLDYN ANGSGAGVTQ FLNNETDFAG SDVPLNPSTG QPDRAAERCG
     SPAWDLPTVF GPIAITYNIK GVSTLNLDGP TTAKIFNGTI TVWNDPQIQA LNSGTDLPPT
     PISVIFRSDK SGTSDNFQKY LDGASNGAWG KGASETFNGG VGVGASGNNG TSALLQTTDG
     SITYNEWSFA VGKQLNMAQI ITSAGPDPVA ITTESVGKTI AGAKIMGQGN DLVLDTSSFY
     RPTQPGSYPI VLATYEIVCS KYPDATTGTA VRAFMQAAIG PGQEGLDQYG SIPLPKSFQA
     KLAAAVNAIS