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LOCUS WP_000193529 328 aa linear BCT 01-JAN-2025 ACCESSION WP_000193529 VERSION WP_000193529.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 328) AUTHORS Wilkens,S. TITLE Structure and mechanism of ABC transporters JOURNAL F1000Prime Rep 7, 14 (2015) PUBMED 25750732 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 328) 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 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 11418519 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..328 /organism="Escherichia coli" /db_xref="taxon:562" Protein 1..328 /product="ABC transporter ATP-binding protein" /GO_function="GO:0016887 - ATP hydrolysis activity [Evidence IEA]" /GO_function="GO:0042626 - ATPase-coupled transmembrane transporter activity [Evidence IEA]" /GO_function="GO:0140359 - ABC-type transporter activity [Evidence IEA]" /calculated_mol_wt=35969 Region 5..325 /region_name="DppD" /note="ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]; COG0444" /db_xref="CDD:440213" ORIGIN 1 mtqpvldiqq lhlsfpgfng dvhalnnvsl qinrgeivgl vgesgsgksv tamlimrllp 61 tgsycvhrgq isllgddvln arekqlrqwr garvamifqe pmtalnptrr iglqmmdvir 121 hhqpisrrea rakaiallee mqipdtvevm srypfelsgg mrqrvmiala fscepqliia 181 depttaldvt vqlqvlrllk hkardsgtav lfishdmavv sqlcdsvyvm yagsviesgv 241 tadvihhprh pytigllqca pehgvprqpl paipgtvpnl thlpdgcafr drcyaagaqc 301 envpaltacg dnnqrcacwy pqqevisv