PstS family phosphate ABC transporter substrate-binding protein

LOCUS       WP_000982774             502 aa            linear   BCT 19-FEB-2025
            [Escherichia coli].
ACCESSION   WP_000982774
VERSION     WP_000982774.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 502)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Diaz,M., Esteban,A., Fernandez-Abalos,J.M. and Santamaria,R.I.
  TITLE     The high-affinity phosphate-binding protein PstS is accumulated
            under high fructose concentrations and mutation of the
            corresponding gene affects differentiation in Streptomyces lividans
  JOURNAL   Microbiology (Reading) 151 (Pt 8), 2583-2592 (2005)
   PUBMED   16079337
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Locher,K.P.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   Curr Opin Struct Biol 14 (4), 426-431 (2004)
   PUBMED   15313236
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Higgins,C.F.
  TITLE     ABC transporters: physiology, structure and mechanism--an overview
  JOURNAL   Res Microbiol 152 (3-4), 205-210 (2001)
   PUBMED   11421269
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..502
                     /product="PstS family phosphate ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56523
     Region          244..497
                     /region_name="PstS"
                     /note="ABC-type phosphate transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG0226"
                     /db_xref="CDD:439996"
ORIGIN      
        1 mmpnrkwilt slimtffgip ilaqflaavv amlgvgltgi ievcnilitp tiylllnvfm
       61 ltlgaiiiff sgrvwagdsa penreiavwr qcffllpall tlvgwiitlh ladyqfrqmg
      121 agwlanlmlp wlgvflvslv ggeywwmvii pvgahisfsl gyawptrypl sgtsglrcrn
      181 lllflllllg ivagyqahly kqqnpgvgvr enidirawrp dklnnrltpl rgkpqiqfrq
      241 nwpridgata aypiyasafy alsvipedfh vweylensrt pdaynrivkg dadiifvaqp
      301 sggqkkraee sgvtllytpf areafvfivn adnpvnslte qqvrdifsga itnwrtvggn
      361 dqeiqtwqrp edsgsqtvmq sqvmkkvrmi spqetevasv megmikvvae yrntnnaigy
      421 tfryyatqmn adknirllai ngitptaeni rngkyayivd afmvtrentt setqklvewf
      481 ltpqgqslve dvgyvplylt me