MULTISPECIES: ABC transporter substrate-binding protein

LOCUS       WP_004151804             372 aa            linear   BCT 26-FEB-2025
            [Klebsiella].
ACCESSION   WP_004151804
VERSION     WP_004151804.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Sebulsky,M.T., Shilton,B.H., Speziali,C.D. and Heinrichs,D.E.
  TITLE     The role of FhuD2 in iron(III)-hydroxamate transport in
            Staphylococcus aureus. Demonstration that FhuD2 binds
            iron(III)-hydroxamates but with minimal conformational change and
            implication of mutations on transport
  JOURNAL   J Biol Chem 278 (50), 49890-49900 (2003)
   PUBMED   14514690
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Borths,E.L., Locher,K.P., Lee,A.T. and Rees,D.C.
  TITLE     The structure of Escherichia coli BtuF and binding to its cognate
            ATP binding cassette transporter
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16642-16647 (2002)
   PUBMED   12475936
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Staudenmaier,H., Van Hove,B., Yaraghi,Z. and Braun,V.
  TITLE     Nucleotide sequences of the fecBCDE genes and locations of the
            proteins suggest a periplasmic-binding-protein-dependent transport
            mechanism for iron(III) dicitrate in Escherichia coli
  JOURNAL   J Bacteriol 171 (5), 2626-2633 (1989)
   PUBMED   2651410
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  :: HMM
            Evidence Accession :: NF013648.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF01497.23
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..372
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=41163
     Region          28..360
                     /region_name="TroA-like"
                     /note="Helical backbone metal receptor (TroA-like domain).
                     These proteins have been shown to function in the ABC
                     transport of ferric siderophores and metal ions such as
                     Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is
                     formed in the interface between...; cl00262"
                     /db_xref="CDD:469696"
     Site            order(139..140,143,170)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238347"
ORIGIN      
        1 marksvrsll ltallatpll syatqypltv tdldgrqvtl akepqriilq dgrdimtlal
       61 ldrdnpfkrl vawnnlakkq dvatwqmlkt twpqsatild mgfsdkgnvd lesviarqpd
      121 lmiaqlrarp almesgvidk lsalhvpvlf vdyeiapakd tapsidllgk vlnresqaka
      181 ftdyyrqqlq sirqktatit pkanvfveal agnsdaccft hghsgwgglv eavgannigs
      241 qllpgasgfv slekiismkp dawimtgskr gnsqvlplgy avkpeavkaq aqtllarpgv
      301 sqipavqekr aygvyhhfyn hpwnivgmey lakdiypqaf gdlnpdetyh yivrhftdlp
      361 dqpfvfswqq se