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LOCUS WP_004189329 352 aa linear BCT 21-JAN-2025 substrate-binding protein [Klebsiella]. ACCESSION WP_004189329 VERSION WP_004189329.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 352) AUTHORS Beis,K. TITLE Structural basis for the mechanism of ABC transporters JOURNAL Biochem Soc Trans 43 (5), 889-893 (2015) PUBMED 26517899 REFERENCE 2 (residues 1 to 352) 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 3 (residues 1 to 352) AUTHORS Dwyer,M.A. and Hellinga,H.W. TITLE Periplasmic binding proteins: a versatile superfamily for protein engineering JOURNAL Curr Opin Struct Biol 14 (4), 495-504 (2004) PUBMED 15313245 REFERENCE 4 (residues 1 to 352) AUTHORS Locher,K.P. TITLE Structure and mechanism of ABC transporters JOURNAL Curr Opin Struct Biol 14 (4), 426-431 (2004) PUBMED 15313236 REFERENCE 5 (residues 1 to 352) AUTHORS Magnusson,U., Salopek-Sondi,B., Luck,L.A. and Mowbray,S.L. TITLE X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity JOURNAL J Biol Chem 279 (10), 8747-8752 (2004) PUBMED 14672931 REFERENCE 6 (residues 1 to 352) AUTHORS Fukami-Kobayashi,K., Tateno,Y. and Nishikawa,K. TITLE Parallel evolution of ligand specificity between LacI/GalR family repressors and periplasmic sugar-binding proteins JOURNAL Mol Biol Evol 20 (2), 267-277 (2003) PUBMED 12598694 REFERENCE 7 (residues 1 to 352) 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 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 10156937 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..352 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..352 /product="branched-chain amino acid ABC transporter substrate-binding protein" /GO_function="GO:0015658 - branched-chain amino acid transmembrane transporter activity [Evidence IEA]" /GO_function="GO:0022857 - transmembrane transporter activity [Evidence IEA]" /GO_function="GO:0140359 - ABC-type transporter activity [Evidence IEA]" /GO_process="GO:0015803 - branched-chain amino acid transport [Evidence IEA]" /GO_process="GO:0055085 - transmembrane transport [Evidence IEA]" /calculated_mol_wt=37537 Region 10..343 /region_name="PBP1_ABC_LIVBP-like" /note="type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine); cd06342" /db_xref="CDD:380565" Site order(84..86,107..108,157,209,233) /site_type="other" /note="ligand binding site [chemical binding]" /db_xref="CDD:380565" ORIGIN 1 mafyaqadvk igvagpftgp natygaqywk gasqavadin aaggikgeki vlvqgddace 61 pkqavavanr lvdeakvsav vghfcssstm pasevydeag iltitpgstn pqitergmkd 121 lfrmcgrddq qgaiaanyml dvlkakkiav ihdkdtygqg ladatraala krgtkevlye 181 glsrgekdfn alvtkigalk pdvvyfggch peagplvrqm reqgvqakff sgdcivteel 241 vtaaggpqft ngvlmtfgqd prtlpdgkav iekfrasgfe pegytlyaya siqaiaaawn 301 avgtdnakas dwlkshdvet vmgkkawdgk gdlkvsdyvv yqwddkgkyh ql