ID   PSTS3_MYCLE             Reviewed;         369 AA.
AC   Q9CBE5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Phosphate-binding protein PstS 3;
DE            Short=PBP 3;
DE            Short=PstS-3;
DE   Flags: Precursor;
GN   Name=pstS2; Synonyms=phoS2; OrderedLocusNames=ML2095;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC       phosphate import. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}.
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DR   EMBL; AL583924; CAC31050.1; -; Genomic_DNA.
DR   PIR; B87171; B87171.
DR   RefSeq; NP_302395.1; NC_002677.1.
DR   RefSeq; WP_010908715.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBE5; -.
DR   SMR; Q9CBE5; -.
DR   STRING; 272631.ML2095; -.
DR   EnsemblBacteria; CAC31050; CAC31050; CAC31050.
DR   KEGG; mle:ML2095; -.
DR   PATRIC; fig|272631.5.peg.3941; -.
DR   Leproma; ML2095; -.
DR   eggNOG; COG0226; Bacteria.
DR   HOGENOM; CLU_034528_0_0_11; -.
DR   OMA; KGPKNDG; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Phosphate transport;
KW   Reference proteome; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..369
FT                   /note="Phosphate-binding protein PstS 3"
FT                   /id="PRO_0000031858"
FT   BINDING         55..57
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         85
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         103
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   BINDING         190..192
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT7"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   369 AA;  37733 MW;  697DECBC6AB4B9AC CRC64;
     MKLNQFGAAI GLLATGALLS GCGSDNNAAV GSARTGPSSG QVSCGGKPTL KASGSTAQAN
     AMTRFVNAFE RSCPGQTLNY TANGSGAGVS EFNGNQTDFG GSDSPLSRKE YAAAEQRCGS
     QAWNLPVVFG PIAITYNVNG LSSLNLDGPT TAKIFNGSIA SWNDPAIQAL NTGVALPAEP
     IHVVFRNDES GTTDNFQRYL DVASNGEWGK GIGKTFKGGV GEGAKGNDGT SAAVKSTEGS
     ITYNEWSFAS ARKLNTAKIA TSADPEPIAI SVDSVGKTIS GATIIGEGND LVLDTVSFYK
     PAQPGSYPIV LATYEIVCSK YPDAQVGRAV KAFLQSTIGG GQNGLGDNGY VPIPDSFKSR
     LSTAANAIA