PSTS2_MYCTU
ID PSTS2_MYCTU Reviewed; 370 AA.
AC P9WGT9; L0T576; O05870; P96905;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Phosphate-binding protein PstS 2;
DE Short=PBP 2;
DE Short=PstS-2;
DE Flags: Precursor;
GN Name=pstS2; OrderedLocusNames=Rv0932c; ORFNames=MTCY08D9.07;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
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).
RN [2]
RP SEQUENCE REVISION TO 361.
RA Content J.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=15731097; DOI=10.1128/iai.73.3.1898-1902.2005;
RA Peirs P., Lefevre P., Boarbi S., Wang X.M., Denis O., Braibant M.,
RA Pethe K., Locht C., Huygen K., Content J.;
RT "Mycobacterium tuberculosis with disruption in genes encoding the phosphate
RT binding proteins PstS1 and PstS2 is deficient in phosphate uptake and
RT demonstrates reduced in vivo virulence.";
RL Infect. Immun. 73:1898-1902(2005).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=20933472; DOI=10.1016/j.tube.2010.09.004;
RA Vanzembergh F., Peirs P., Lefevre P., Celio N., Mathys V., Content J.,
RA Kalai M.;
RT "Effect of PstS sub-units or PknD deficiency on the survival of
RT Mycobacterium tuberculosis.";
RL Tuberculosis 90:338-345(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Functions in inorganic phosphate uptake, although probably
CC not the main uptake protein under phosphate starvation
CC (PubMed:15731097, PubMed:20933472). Part of the ABC transporter complex
CC PstSACB involved in phosphate import (Probable).
CC {ECO:0000269|PubMed:15731097, ECO:0000269|PubMed:20933472,
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:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: Transcription not induced by phosphate starvation, protein
CC levels do not increase either (at protein level). Part of the pstS2-
CC pknD operon. {ECO:0000269|PubMed:20933472}.
CC -!- DISRUPTION PHENOTYPE: No growth phenotype in phosphate-rich medium (3.6
CC mM Pi) (PubMed:15731097). In restricted medium (Sauton) grows better
CC than wild-type even after nutrient starvation (PubMed:20933472).
CC Decreased phosphate uptake in phosphate-depleted medium
CC (PubMed:15731097). Decreased growth in infected BALB/c and C57BL/6 mice
CC for up to 5 months after infection (PubMed:15731097).
CC {ECO:0000269|PubMed:15731097, ECO:0000269|PubMed:20933472}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR EMBL; Z48056; CAA88137.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43680.1; -; Genomic_DNA.
DR PIR; D70584; D70584.
DR RefSeq; WP_003898652.1; NZ_NVQJ01000001.1.
DR RefSeq; YP_177769.1; NC_000962.3.
DR AlphaFoldDB; P9WGT9; -.
DR SMR; P9WGT9; -.
DR STRING; 83332.Rv0932c; -.
DR PaxDb; P9WGT9; -.
DR DNASU; 885613; -.
DR GeneID; 885613; -.
DR KEGG; mtu:Rv0932c; -.
DR TubercuList; Rv0932c; -.
DR eggNOG; COG0226; Bacteria.
DR OMA; QFVYAYI; -.
DR PhylomeDB; P9WGT9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
DR GO; GO:0006817; P:phosphate ion transport; IMP:MTBBASE.
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 Reference proteome; Signal; Transport; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..370
FT /note="Phosphate-binding protein PstS 2"
FT /id="PRO_0000031855"
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; 37864 MW; 97F5116CEE9B3B5C CRC64;
MKFARSGAAV SLLAAGTLVL TACGGGTNSS SSGAGGTSGS VHCGGKKELH SSGSTAQENA
MEQFVYAYVR SCPGYTLDYN ANGSGAGVTQ FLNNETDFAG SDVPLNPSTG QPDRSAERCG
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
