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LOCUS WP_001032214 330 aa linear BCT 19-FEB-2025 substrate-binding protein [Enterobacteriaceae]. ACCESSION WP_001032214 VERSION WP_001032214.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 330) 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 330) 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 330) 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 330) 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 330) 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 330) 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 330) 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 330) 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 330) 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 330) 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..330 /organism="Enterobacteriaceae" /db_xref="taxon:543" Protein 1..330 /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=36990 Region 59..323 /region_name="PstS" /note="ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism]; COG0226" /db_xref="CDD:439996" ORIGIN 1 mnkftgvlll gtallagcvd regyynsvre eeshgltslr gqpalrysdd wsrwprvyga 61 talyplyasa yyklvpepkd kdrtslawqa yglqqtrtae aydslikgsa tvifvaqpse 121 gqkkraeeag vklkytafar eafvfivdin npvnslsehq vkdifsgkts rwnkvggsde 181 hikvwqrped sgsqtimkgl vmqdtpmlpa kkstvidlmg glitevadyq ntpssigytf 241 hyyvtrmndn mlkmrkqikl laingvapte enirngtypy ivdaymvtre nptpetqkfv 301 dwfisqqgqq lvedvgyvpl yeaspessgq