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LOCUS WP_000194222 452 aa linear BCT 23-DEC-2024 ACCESSION WP_000194222 VERSION WP_000194222.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 452) AUTHORS Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P. TITLE Understanding transport by the major facilitator superfamily (MFS): structures pave the way JOURNAL Nat Rev Mol Cell Biol 17 (2), 123-132 (2016) PUBMED 26758938 REFERENCE 2 (residues 1 to 452) AUTHORS Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D. TITLE Energy coupling mechanisms of MFS transporters JOURNAL Protein Sci 24 (10), 1560-1579 (2015) PUBMED 26234418 REFERENCE 3 (residues 1 to 452) AUTHORS Yan,N. TITLE Structural Biology of the Major Facilitator Superfamily Transporters JOURNAL Annu Rev Biophys 44, 257-283 (2015) PUBMED 26098515 REFERENCE 4 (residues 1 to 452) AUTHORS Yan,N. TITLE Structural advances for the major facilitator superfamily (MFS) transporters JOURNAL Trends Biochem Sci 38 (3), 151-159 (2013) PUBMED 23403214 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 13024277 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..452 /organism="Salmonella" /db_xref="taxon:590" Protein 1..452 /product="MFS transporter" /GO_component="GO:0016020 - membrane [Evidence IEA]" /GO_function="GO:0022857 - transmembrane transporter activity [Evidence IEA]" /GO_process="GO:0055085 - transmembrane transport [Evidence IEA]" /calculated_mol_wt=48186 Region 24..430 /region_name="MFS_PcaK_like" /note="4-hydroxybenzoate transporter PcaK and similar transporters of the Major Facilitator Superfamily; cd17365" /db_xref="CDD:340923" Site order(34..35,38..39,42,74,124..125,127..129,132,152, 155..156,159,263,266..267,270..272,275,302,306,356..357, 361,365,381,384..385,388..389,392) /site_type="other" /note="putative chemical substrate binding pocket [chemical binding]" /db_xref="CDD:340923" ORIGIN 1 mtqrrdlqal idaapvgkmq wrviiccflv vmldgfdtaa igfiapdirt hwqlsasela 61 plfgagllgl tagallcgpl adrfgrkrvi elcvalfgal sllsafspdi etlvllrflt 121 glglggampn titmtseylp arrrgalvtl mfcgftlgsa mggivsaqlv pligwhgila 181 lggilplmlf fgllfalpes prwqvrrqlp qavvartvsa itgeryhdtq fflhetaava 241 kgsirqlfag rqlvitlmlw vvffmsllii yllsswmptl lnhrgidlqq aswvtaafqv 301 ggtlgalllg vlmdrlnpfr vlavsyalga vcivmiglse nglwlmalai fgtgigisgs 361 qvglnaltat lyptqsratg vswsnaigrc gaivgslsgg mmmalnfsfd tlffviaipa 421 aisavmltll tvvvrlsisv pddlprasvv ne