ID   MALT_SALDC              Reviewed;         902 AA.
AC   B5FKD6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=HTH-type transcriptional regulator MalT {ECO:0000255|HAMAP-Rule:MF_01247};
DE   AltName: Full=ATP-dependent transcriptional activator MalT {ECO:0000255|HAMAP-Rule:MF_01247};
GN   Name=malT {ECO:0000255|HAMAP-Rule:MF_01247}; OrderedLocusNames=SeD_A3885;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Positively regulates the transcription of the maltose regulon
CC       whose gene products are responsible for uptake and catabolism of malto-
CC       oligosaccharides. Specifically binds to the promoter region of its
CC       target genes, recognizing a short DNA motif called the MalT box.
CC       {ECO:0000255|HAMAP-Rule:MF_01247}.
CC   -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are both
CC       required for DNA binding. {ECO:0000255|HAMAP-Rule:MF_01247}.
CC   -!- SUBUNIT: Monomer in solution. Oligomerizes to an active state in the
CC       presence of the positive effectors ATP and maltotriose.
CC       {ECO:0000255|HAMAP-Rule:MF_01247}.
CC   -!- SIMILARITY: Belongs to the MalT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01247}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001144; ACH74410.1; -; Genomic_DNA.
DR   RefSeq; WP_000907032.1; NC_011205.1.
DR   AlphaFoldDB; B5FKD6; -.
DR   SMR; B5FKD6; -.
DR   KEGG; sed:SeD_A3885; -.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   Proteomes; UP000008322; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045913; P:positive regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   HAMAP; MF_01247; HTH_type_MalT; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR041617; TPR_MalT.
DR   InterPro; IPR023768; Tscrpt_reg_HTH_MalT.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Carbohydrate metabolism; DNA-binding;
KW   Nucleotide-binding; Transcription; Transcription regulation.
FT   CHAIN           1..902
FT                   /note="HTH-type transcriptional regulator MalT"
FT                   /id="PRO_1000139854"
FT   DOMAIN          830..895
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
FT   DNA_BIND        854..873
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
SQ   SEQUENCE   902 AA;  103144 MW;  AD9BC6D63088E99C CRC64;
     MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALVTSP AGYGKTTLVS QWAAGKNELG
     WYSLDEGDNQ QERFASYLIA AIQQATGGHC STSEAMAQKR QYASLTSLFA QLFIELAQWH
     RPLYLVIDDY HLITNPVIHD AMRFFLRHQP ENFTLVVLSR NLPQLGIANL RVRDQLLEIG
     SQQLAFNHQE AKQFFDRRLS SPIEAAESSR MCDDVAGWAT ALQLIALSAR QNHTSAHHSA
     RRLAGINASH LSDYLVDEVL DNVDVSTRHF LLKSAILRSM NDALIVRVTG EENGQMRLEE
     IERQGLFLQR MDDTGEWFSY HPLFGSFLRQ RCQWELAAEL PEIHRAAAES WMEQGFPSEA
     IHHALAAGDA QMLRDILLNH AWGLFNHSEL ALLEESLKAL PWESLLENPR LVLLQAWLMQ
     SQHRYSEVNT LLARAEQEIK GVMDGTLHAE FNALRAQVAI NDGNPEEAER LAKLALDELP
     LAWFYSRIVA TSVHGEVLHC KGDLSQSLSL MQQTEQMARH HDVWHYALWS LIQQSEIQFA
     QGFLQAAWET QERAFQLIKE QQHLEQLPMH EFLVRIRAQL LWAWARLDEA EASARSGIAV
     LSTFQPQQQL QCLTLLVQCS LARGDLDNAR SQLNRLENLL GNGRYHCDWI SNADKVRVIY
     WQLTGDKKSA ANWLRHTPKP AFANNHFLQG QWRNIARAQI LLGEFEPAEI VLEELNENAR
     SLRLMSDLNR NLLLLNQLYW QSGRKNDAQR VLLDALQLAN RTGFISHFVI EGEAMAQQLR
     QLIQLNTLPE MEQHRAQRIL REINQHHRHK FAHFDEGFVE RLLNHPDVPE LIRTSPLTQR
     EWQVLGLIYS GYSNEQIAGE LAVAATTIKT HIRNLYQKLG VAHRQDAVQH AQQLLKMMGY
     GV