ID   MALT_ECODH              Reviewed;         901 AA.
AC   B1X764;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=ECDH10B_3593;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB04476.1; -; Genomic_DNA.
DR   RefSeq; WP_000906961.1; NC_010473.1.
DR   AlphaFoldDB; B1X764; -.
DR   EMDB; EMD-16140; -.
DR   SMR; B1X764; -.
DR   KEGG; ecd:ECDH10B_3593; -.
DR   HOGENOM; CLU_006325_3_0_6; -.
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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR023768; Tscrpt_reg_HTH_MalT.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR44688; -; 1.
DR   PANTHER; PTHR44688:SF7; HTH-TYPE TRANSCRIPTIONAL REGULATOR MALT; 1.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 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_1000139847"
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;  103118 MW;  9B27CE0F632AD417 CRC64;
     MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALITSP AGYGKTTLIS QWAAGKNDIG
     WYSLDEGDNQ QERFASYLIA AVQQATNGHC AICETMAQKR QYASLTSLFA QLFIELAEWH
     SPLYLVIDDY HLITNPVIHE SMRFFIRHQP ENLTLVVLSR NLPQLGIANL RVRDQLLEIG
     SQQLAFTHQE AKQFFDCRLS SPIEAAESSR ICDDVSGWAT ALQLIALSAR QNTHSAHKSA
     RRLAGINASH LSDYLVDEVL DNVDLATRHF LLKSAILRSM NDALITRVTG EENGQMRLEE
     IERQGLFLQR MDDTGEWFCY HPLFGNFLRQ RCQWELAAEL PEIHRAAAES WMAQGFPSEA
     IHHALAAGDA LMLRDILLNH AWSLFNHSEL SLLEESLKAL PWDSLLENPQ LVLLQAWLMQ
     SQHRYGEVNT LLARAEHEIK DIREDTMHAE FNALRAQVAI NDGNPDEAER LAKLALEELP
     PGWFYSRIVA TSVLGEVLHC KGELTRSLAL MQQTEQMARQ HDVWHYALWS LIQQSEILFA
     QGFLQTAWET QEKAFQLINE QHLEQLPMHE FLVRIRAQLL WAWARLDEAE ASARSGIEVL
     SSYQPQQQLQ CLAMLIQCSL ARGDLDNARS QLNRLENLLG NGKYHSDWIS NANKVRVIYW
     QMTGDKAAAA NWLRHTAKPE FANNHFLQGQ WRNIARAQIL LGEFEPAEIV LEELNENARS
     LRLMSDLNRN LLLLNQLYWQ AGRKSDAQRV LLDALKLANR TGFISHFVIE GEAMAQQLRQ
     LIQLNTLPEL EQHRAQRILR EINQHHRHKF AHFDENFVER LLNHPEVPEL IRTSPLTQRE
     WQVLGLIYSG YSNEQIAGEL EVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
     V
//