PSTS3_MYCTU
ID PSTS3_MYCTU Reviewed; 370 AA.
AC P9WGT7; L0T5B5; O86343; P0A5Y2; Q50794;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Phosphate-binding protein PstS 3;
DE Short=PBP 3;
DE Short=PstS-3;
DE AltName: Full=Antigen Ag88;
DE Flags: Precursor;
GN Name=pstS3; Synonyms=phoS2; OrderedLocusNames=Rv0928;
GN ORFNames=MTCY21C12.22;
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].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=8843165; DOI=10.1016/0014-5793(96)00953-2;
RA Braibant M., Lefevre P., de Wit L., Ooms J., Peirs P., Huygen K.,
RA Wattiez R., Content J.;
RT "Identification of a second Mycobacterium tuberculosis gene cluster
RT encoding proteins of an ABC phosphate transporter.";
RL FEBS Lett. 394:206-212(1996).
RN [2]
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 [3]
RP 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Beijing GC1237;
RX PubMed=20844580; DOI=10.1371/journal.ppat.1001100;
RA Brodin P., Poquet Y., Levillain F., Peguillet I., Larrouy-Maumus G.,
RA Gilleron M., Ewann F., Christophe T., Fenistein D., Jang J., Jang M.S.,
RA Park S.J., Rauzier J., Carralot J.P., Shrimpton R., Genovesio A.,
RA Gonzalo-Asensio J.A., Puzo G., Martin C., Brosch R., Stewart G.R.,
RA Gicquel B., Neyrolles O.;
RT "High content phenotypic cell-based visual screen identifies Mycobacterium
RT tuberculosis acyltrehalose-containing glycolipids involved in phagosome
RT remodeling.";
RL PLoS Pathog. 6:E1001100-E1001100(2010).
RN [5]
RP FUNCTION, INDUCTION BY PHOSPHATE STARVATION, 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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, AND
RP SUBUNIT.
RX PubMed=24615888; DOI=10.1002/prot.24548;
RA Ferraris D.M., Spallek R., Oehlmann W., Singh M., Rizzi M.;
RT "Crystal structure of the Mycobacterium tuberculosis phosphate binding
RT protein PstS3.";
RL Proteins 82:2268-2274(2014).
CC -!- FUNCTION: Functions in inorganic phosphate uptake, is probably the main
CC carrier for phosphate uptake, it is the most highly expressed of the 3
CC PstS proteins under phosphate starvation (PubMed:20933472). Binds
CC phosphate; probably able to bind both H(2)PO(4)(-) and HPO(4)(2-)
CC (PubMed:24615888). Part of the ABC transporter complex PstSACB involved
CC in phosphate import (Probable). Probably plays a role in host phagosome
CC maturation arrest (PubMed:20844580). {ECO:0000269|PubMed:20933472,
CC ECO:0000269|PubMed:24615888, ECO:0000305, ECO:0000305|PubMed:20844580}.
CC -!- SUBUNIT: Monomer (PubMed:24615888). The complex is composed of two ATP-
CC binding proteins (PstB), two transmembrane proteins (PstC and PstA) and
CC a solute-binding protein (PstS). {ECO:0000269|PubMed:24615888,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: Transcription induced 6-fold by phosphate starvation,
CC protein levels increase after 24 hours starvation (at protein level)
CC (PubMed:20933472). Part of the pstS3-pstC2-pstA1 operon.
CC {ECO:0000269|PubMed:20844580, ECO:0000269|PubMed:20933472}.
CC -!- DISRUPTION PHENOTYPE: Grows normally in liquid culture, traffics into
CC host (human and mouse) acidified compartments early after phagocytosis,
CC suggesting it no longer arrests phagosome maturation as well as wild-
CC type, impaired growth in mouse macrophages (PubMed:20844580). No growth
CC phenotype in phosphate-rich medium (3.6 mM Pi), nor in restricted
CC medium (Sauton), but in phosphate-free Sauton medium dies faster than
CC wild-type when pre-exposed to complete starvation (PubMed:20933472).
CC {ECO:0000269|PubMed:20933472}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z48057; CAA88138.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43676.1; -; Genomic_DNA.
DR PIR; H70583; H70583.
DR RefSeq; WP_003404775.1; NZ_NVQJ01000001.1.
DR RefSeq; YP_177768.1; NC_000962.3.
DR PDB; 4LVQ; X-ray; 2.30 A; A/B=1-370.
DR PDBsum; 4LVQ; -.
DR AlphaFoldDB; P9WGT7; -.
DR SMR; P9WGT7; -.
DR STRING; 83332.Rv0928; -.
DR PaxDb; P9WGT7; -.
DR DNASU; 885366; -.
DR GeneID; 45424894; -.
DR GeneID; 885366; -.
DR KEGG; mtu:Rv0928; -.
DR TubercuList; Rv0928; -.
DR eggNOG; COG0226; Bacteria.
DR OMA; KGPKNDG; -.
DR PhylomeDB; P9WGT7; -.
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:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0051301; P:cell division; IDA:MTBBASE.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IDA:MTBBASE.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
DR GO; GO:0052170; P:suppression by symbiont of host innate immune response; IDA: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 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphate transport; Reference proteome; Signal; Stress response;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..370
FT /note="Phosphate-binding protein PstS 3"
FT /id="PRO_0000031859"
FT BINDING 56..58
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:24615888"
FT BINDING 86
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:24615888"
FT BINDING 104
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000305|PubMed:24615888"
FT BINDING 191..193
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:24615888"
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"
FT VARIANT 112..114
FT /note="AAA -> PSG (in strain: Erdman)"
FT VARIANT 116
FT /note="Q -> A (in strain: Erdman)"
FT VARIANT 118
FT /note="Missing (in strain: Erdman)"
FT VARIANT 253..254
FT /note="QH -> HD (in strain: Erdman)"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 123..137
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4LVQ"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4LVQ"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:4LVQ"
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
