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 27-MAR-2024, entry version 32.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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 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 CDD; cd13565; PBP2_PstS; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005673; ABC_phos-bd_PstS.
DR InterPro; IPR024370; PBP_domain.
DR NCBIfam; TIGR00975; 3a0107s03; 1.
DR PANTHER; PTHR42996; PHOSPHATE-BINDING PROTEIN PSTS; 1.
DR PANTHER; PTHR42996:SF1; PHOSPHATE-BINDING PROTEIN PSTS; 1.
DR Pfam; PF12849; PBP_like_2; 1.
DR PIRSF; PIRSF002756; PstS; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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
//
