ID   PSTS3_MYCBP             Reviewed;         370 AA.
AC   A0A0H3MBK5;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Phosphate-binding protein PstS3 {ECO:0000303|PubMed:9139906};
DE            Short=PstS-3;
DE   AltName: Full=38-kDa lipoprotein;
DE            Short=P38;
DE   Flags: Precursor;
GN   Name=pstS3; OrderedLocusNames=BCG_0980;
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, is probably the main
CC       carrier for phosphate uptake (By similarity). Part of the ABC
CC       transporter complex PstSACB involved in phosphate import (Probable).
CC       {ECO:0000250|UniProtKB:P9WGT7, 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; CAL70966.1; -; Genomic_DNA.
DR   RefSeq; WP_003404775.1; NC_008769.1.
DR   AlphaFoldDB; A0A0H3MBK5; -.
DR   SMR; A0A0H3MBK5; -.
DR   GeneID; 45424894; -.
DR   KEGG; mbb:BCG_0980; -.
DR   HOGENOM; CLU_034528_0_0_11; -.
DR   OMA; KGPKNDG; -.
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 PstS3"
FT                   /id="PRO_5002615476"
FT   BINDING         56..58
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         86
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         104
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;  37953 MW;  7D557829A9A118E0 CRC64;
     MKLNRFGAAV GVLAAGALVL SACGNDDNVT GGGATTGQAS AKVDCGGKKT LKASGSTAQA
     NAMTRFVNVF EQACPGQTLN YTANGSGAGI SEFNGNQTDF GGSDVPLSKD EAAAAQRRCG
     SPAWNLPVVF GPIAVTYNLN SVSSLNLDGP TLAKIFNGSI TQWNNPAIQA LNRDFTLPGE
     RIHVVFRSDE SGTTDNFQRY LQAASNGAWG KGAGKSFQGG VGEGARGNDG TSAAAKNTPG
     SITYNEWSFA QAQHLTMANI VTSAGGDPVA ITIDSVGQTI AGATISGVGN DLVLDTDSFY
     RPKRPGSYPI VLATYEIVCS KYPDSQVGTA VKAFLQSTIG AGQSGLGDNG YIPIPDEFKS
     RLSTAVNAIA