ID   PSTS3_MYCAV             Reviewed;         369 AA.
AC   Q9KK89;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Phosphate-binding protein PstS 3;
DE            Short=PBP 3;
DE            Short=PstS-3;
DE   Flags: Precursor;
GN   Name=pstS3;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=969A45;
RX   PubMed=10970760; DOI=10.1054/tuld.2000.0239;
RA   Carroll J.D., Wallace R.C., Keane J., Remold H.G., Arbeit R.D.;
RT   "Identification of Mycobacterium avium DNA sequences that encode exported
RT   proteins by using phoA gene fusions.";
RL   Tuber. Lung Dis. 80:117-130(2000).
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; AF137360; AAF74819.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KK89; -.
DR   SMR; Q9KK89; -.
DR   PRIDE; Q9KK89; -.
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   Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..369
FT                   /note="Phosphate-binding protein PstS 3"
FT                   /id="PRO_0000031856"
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           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   369 AA;  37226 MW;  CB0EA0AC10F463EC CRC64;
     MKLNRFGAVL SVLSAGALVL SGCGSDNNGA GAGAAGSSSS KVSCGGKKAL KASGSTAQAN
     AMTRFVNAFE QACPGQTLNY TANGSGAGIS EFNGKQTDFG GSDSPLAPSE YAAAQQRCGS
     PAWNLPVVFG PIAITYNVAG LNSLNLDGAT AAKIFNGAIT TWNDPGIQAL NPGVALPAEP
     IHVVFRNDES GTTDNFQKYL DAAADGAWGK GAGKTFKGGV GEGAKGNDGT SAAIKATEGS
     ITYNEWSFAQ AQKLNMAKII TSAGPDAVAI SADSVGKTIA GAKISGQGND LVLDTLSFYK
     PTQAGSYPIV LATYEIVCSK YPDPQVGTAV KAFLQSTVGA GQNGLADNGY IPIPDAFKSR
     LSAAINAIT