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ABC transporter substrate-binding protein [Photobacterium


LOCUS       WP_008989760             344 aa            linear   BCT 20-JAN-2025
            leiognathi].
ACCESSION   WP_008989760
VERSION     WP_008989760.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium leiognathi
  ORGANISM  Photobacterium leiognathi
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 344)
  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 344)
  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 344)
  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 344)
  AUTHORS   Igarashi,K., Ito,K. and Kashiwagi,K.
  TITLE     Polyamine uptake systems in Escherichia coli
  JOURNAL   Res Microbiol 152 (3-4), 271-278 (2001)
   PUBMED   11421274
REFERENCE   5  (residues 1 to 344)
  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   6  (residues 1 to 344)
  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 11430824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Photobacterium leiognathi"
                     /db_xref="taxon:553611"
     Protein         1..344
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0019808 - polyamine binding [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:0015846 - polyamine transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39369
     Region          2..343
                     /region_name="PotD"
                     /note="Spermidine/putrescine-binding periplasmic protein
                     [Amino acid transport and metabolism]; COG0687"
                     /db_xref="CDD:440451"
ORIGIN      
        1 mkkvfkgvtt ltfaltafnv saenvvlniy nwaeymptdv iqafekeynv tvnystfdnn
       61 eamytklkll dnkgydvvfa styfiekmar egmlakidkt kmhhlkdvyp gllgqqfdpk
      121 ndyslpyvwg vtgisynsds ikndqvtgwn dlwnsdfqrq vmllddvrdv fgmalkaqgh
      181 sinstneaei kqayeklrdl rpnvvvynsd aphvpyvtge amlgmqwngn aylakqempe
      241 lkfvypkegs ilwmdnfivp egsankdlaf kfidffmrpe nqaklveelg fpapnkqaks
      301 flpkvlqndp mifptdeein kgeftndvgd avniyqkywq llks