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LOCUS WP_014343159 325 aa linear BCT 02-MAR-2025 ACCESSION WP_014343159 VERSION WP_014343159.1 KEYWORDS RefSeq. SOURCE Klebsiella pneumoniae ORGANISM Klebsiella pneumoniae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella; Klebsiella pneumoniae complex. REFERENCE 1 (residues 1 to 325) 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 325) 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 325) 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..325 /organism="Klebsiella pneumoniae" /db_xref="taxon:573" Protein 1..325 /product="ABC transporter substrate-binding protein" /calculated_mol_wt=35799 Region 46..307 /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(132..133,136,159) /site_type="other" /note="intersubunit interface [polypeptide binding]" /db_xref="CDD:238347" ORIGIN 1 mpfnqegrmr wfvslllllt gavsaaapqt qtfaddlgrt vtvplhpqri vsmhdlditi 61 plielgappi ashgrtrpdg shylrssaql tgvdfdnsdi rfigtadidl eavaaarpdl 121 iitepsrhvs veqlekiapt vsidhlqgsa peiyrklaql tgtqprlail erryqeqikq 181 lkamvnppqy svsviqanng kvtvhhsyha lgrvlrdagf rfpplierip dgqridvsae 241 qlpeldadfv fatwrsdtgg kpqdelqame gvmpgwcdfm racrtghyil lpreevisns 301 yaalslmvaq vqshiagrpi paeak