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LOCUS WP_000488238 333 aa linear BCT 10-FEB-2020 [Shigella flexneri]. ACCESSION WP_000488238 VERSION WP_000488238.1 KEYWORDS RefSeq. SOURCE Shigella flexneri ORGANISM Shigella flexneri Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella. REFERENCE 1 (residues 1 to 333) AUTHORS Eichhorn,E., van der Ploeg,J.R. and Leisinger,T. TITLE Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems JOURNAL J. Bacteriol. 182 (10), 2687-2695 (2000) PUBMED 10781534 REFERENCE 2 (residues 1 to 333) AUTHORS Hryniewicz,M., Sirko,A., Palucha,A., Bock,A. and Hulanicka,D. TITLE Sulfate and thiosulfate transport in Escherichia coli K-12: identification of a gene encoding a novel protein involved in thiosulfate binding JOURNAL J. Bacteriol. 172 (6), 3358-3366 (1990) PUBMED 2188959 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 :: NBR011171 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..333 /organism="Shigella flexneri" /db_xref="taxon:623" gene 1..333 /gene="ssuA" Protein 1..333 /product="aliphatic sulfonate ABC transporter substrate-binding protein SsuA" /calculated_mol_wt=36145 Region 15..327 /region_name="PRK11553" /note="alkanesulfonate transporter substrate-binding subunit; Provisional" /db_xref="CDD:236929" Site order(49,80,125,149,154,196..197,200,224) /site_type="other" /note="chemical substrate binding site [chemical binding]" /db_xref="CDD:270275" ORIGIN 1 mfrfltfclc evmpmrniik lalagllsvs tfavaaessp ealrigyqkg sigmvlaksh 61 qllekrypqs kiswvefpag pqmlealnvg sidlgstgdi ppifaqaaga dlvyvgvepp 121 kpkaevilva enspiktvad lkghkvafqk gssshnlllr alrqaglkft diqptyltpa 181 daraafqqgn vdawaiwdpy ysaallqggv rvlkdgtdln qtgsfylaar pyaekngafi 241 qgvlatfsea daltrsqreq siallaktmg lpapviasyl dhrppttikp vnaevaalqq 301 qtadlfyenr lvpkkvdirq riwqptqleg kql