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LOCUS WP_010989509 306 aa linear BCT 21-AUG-2024 ACCESSION WP_010989509 VERSION WP_010989509.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 306) 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 306) 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 306) 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 :: NF013648.5 Evidence Source :: EMBL-EBI Source Identifier :: PF01497.23 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..306 /organism="Listeria monocytogenes" /db_xref="taxon:1639" Protein 1..306 /product="ABC transporter substrate-binding protein" /calculated_mol_wt=33431 Region 48..289 /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(125..126,129,151) /site_type="other" /note="intersubunit interface [polypeptide binding]" /db_xref="CDD:238347" ORIGIN 1 myqkhkwaai lmtvllavvl tacgsssdkd sskekesatk tvtdttdrkv evpttpkriv 61 alqnvsemei lgvkpvgttd yyittypdat kgtesvgndk psiekianlk pdliiisdyq 121 kdllenlekv apvyithfgd tpdkqlsnia nllnkkaeke kwdkdyaass keakatlkda 181 gvanekaavi qfygkeiyvh dakvfdglys gagftptdaa kanketkais seaipeyaag 241 adrlfilmpa dgntdsvdem lkgvwkdipa vkknqvykvd ntkwsdysaa aqlyqmedav 301 kqitgk