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LOCUS WP_005046782 237 aa linear BCT 17-NOV-2023 ACCESSION WP_005046782 VERSION WP_005046782.1 KEYWORDS RefSeq. SOURCE Shigella ORGANISM Shigella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 237) AUTHORS Touze,T., Tran,A.X., Hankins,J.V., Mengin-Lecreulx,D. and Trent,M.S. TITLE Periplasmic phosphorylation of lipid A is linked to the synthesis of undecaprenyl phosphate JOURNAL Mol Microbiol 67 (2), 264-277 (2008) PUBMED 18047581 REFERENCE 2 (residues 1 to 237) AUTHORS Tatar,L.D., Marolda,C.L., Polischuk,A.N., van Leeuwen,D. and Valvano,M.A. TITLE An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in undecaprenyl phosphate recycling JOURNAL Microbiology (Reading) 153 (Pt 8), 2518-2529 (2007) PUBMED 17660416 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 :: BlastRule Evidence Accession :: NBR008082 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..237 /organism="Shigella" /db_xref="taxon:620" gene 1..237 /gene="lpxT" Protein 1..237 /product="Kdo(2)-lipid A phosphotransferase" /EC_number="2.7.4.29" /calculated_mol_wt=26662 Region 98..210 /region_name="acidPPc" /note="Acid phosphatase homologues; smart00014" /db_xref="CDD:214471" Site order(110,117,148..150,184,190,194) /site_type="active" /db_xref="CDD:238813" ORIGIN 1 miknlpqivl lnivgpalfl swyipvnhgf wlpidadify ffnqklvesk aflwlvaltn 61 nrafdgcsll amgmlmlsfw lkenapgrrr ivimglvmll tavvlnqlgq alipvkrasp 121 tltftdinrv sellsvptkd asrdsfpgdh gmmllifsaf mwryfgkvag lialiifmvf 181 afprvmigah wftdiivgsm tviliglpwv lltplsdrli tffdkslpgk nkhfqnk