ID   MALT_SALTI              Reviewed;         901 AA.
AC   Q8Z227; Q83ST6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
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};
GN   OrderedLocusNames=STY4281, t3991;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD08099.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71461.1; -; Genomic_DNA.
DR   RefSeq; NP_458389.1; NC_003198.1.
DR   RefSeq; WP_000907046.1; NZ_WSUR01000001.1.
DR   AlphaFoldDB; Q8Z227; -.
DR   SMR; Q8Z227; -.
DR   STRING; 220341.16505078; -.
DR   EnsemblBacteria; AAO71461; AAO71461; t3991.
DR   KEGG; stt:t3991; -.
DR   KEGG; sty:STY4281; -.
DR   PATRIC; fig|220341.7.peg.4375; -.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   Gene3D; 3.40.50.300; -; 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..901
FT                   /note="HTH-type transcriptional regulator MalT"
FT                   /id="PRO_0000184167"
FT   DOMAIN          829..894
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
FT   DNA_BIND        853..872
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"
FT   CONFLICT        67
FT                   /note="G -> S (in Ref. 2; AAO71461)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   901 AA;  103105 MW;  FBE31E1C32BD265B CRC64;
     MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLLLVTSP 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 KGNLSQSLSL MQQTEQMARH HDVWHYALWS LIQQSEIQFA
     QGFLQAAWET QERAFQLIKE QHLEQLPMHE FLVRIRAQLL WAWARLDEAE ASARSGIAVL
     STFQPQQQLQ CLTLLVQCSL ARGDLDNARS QLNRLEKLLG NGRYHCDWIS NADKVRVIYW
     QLTGDKKSAA NWLRHTPKPA FANNHFLQGQ WRNIARAQIL LGEFEPAEIV LEELNENARS
     LRLMSDLNRN LLLLNQLYWQ SGRKNDAQRV LLDALQLANR TGFISHFVIE GEAMAQQLRQ
     LIQLNTLPEM EQHRAQRILR YINQHHRHKF AHFDEGFVER LLNHPDVPEL IRTSPLTQRE
     WQVLGLIYSG YSNEQIAGEL AVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
     V