ID   MALT_ENT38              Reviewed;         901 AA.
AC   A4WFK6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Ent638_3831;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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}.
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DR   EMBL; CP000653; ABP62486.1; -; Genomic_DNA.
DR   RefSeq; WP_015960791.1; NC_009436.1.
DR   AlphaFoldDB; A4WFK6; -.
DR   SMR; A4WFK6; -.
DR   STRING; 399742.Ent638_3831; -.
DR   PRIDE; A4WFK6; -.
DR   EnsemblBacteria; ABP62486; ABP62486; Ent638_3831.
DR   KEGG; ent:Ent638_3831; -.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000000230; 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_1000085771"
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"
SQ   SEQUENCE   901 AA;  103261 MW;  F9DEB83E3F1C1370 CRC64;
     MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALITSP AGYGKTTLIS QWASGKSDLG
     WYSLDEGDNQ TERFASYLIA AIQQATNGHC VTSEIMVQKR QYASLSSLFA QLFIELAEWH
     RPLYLVIDDY HLITNPVIHE SMRFFLRHQP ENLTLVVLSR NLPQLGIANL RVRDQLLEVG
     SQQLSFNHQE AKQFFDCRLS SPIEAAESSR LCDDVAGWAT ALQLIALSAR QNNSPTHQSA
     RRLSGINASH LSDYLVDEVL DSVDPATRQF LLKSSLLRSM NDALIVRVTG EDNGQMRLEE
     IERQGLFLQR MDDSGEWFSF HPLFGSFLRQ RCQWELATEL PEVHRSAAES WMAQGFPSEA
     IHHALAAGDA NMLRDILLNH AWGLFNHSEL TLLEESLRAL PWESLLENPR LVLLQAWLMQ
     SQHRYSEVNM LLARAEQEMK GEMDPTLHGE FNALRAQVAI NDGDPEEAER LAMIALDELP
     LANFYSRIVA TSVHGEVLHC KGDLSRSLAL MQQTEQMARR HDIWHYALWS MIQQSEILFA
     QGFLQAAWET QEKAFQLIHD QHLEQLPMHE FLLRIRAQLL WAWSRLDEAE SSARHGVEVL
     SAFQPQQQLQ CLALLVQCSL ARGDLDNARN HLNRLENLLG NGQYHSDWVS NADKVRVIYW
     QMIGDKKSAA NWLRQTPKPE FANNHFLQSQ WRNIARVQIL LGDFDPAEIV LEELNENARS
     LRLMSDLNRN LLLLNQLYWQ AGRKNDAQRV LLEALQLANR TGFISHFVIE GEVMAQQLRQ
     LIQLNTLPEL DQHRAQRILR EINQHHRHKF AHFDENFVER LLTHPEVPEL IRTSPLTQRE
     WQVLGLIYSG YSNEQIAGEL AVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
     V