ID   MALT_ESCF3              Reviewed;         901 AA.
AC   B7LSC1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=EFER_3387;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ90864.1; -; Genomic_DNA.
DR   RefSeq; WP_000907019.1; NC_011740.1.
DR   AlphaFoldDB; B7LSC1; -.
DR   SMR; B7LSC1; -.
DR   EnsemblBacteria; CAQ90864; CAQ90864; EFER_3387.
DR   KEGG; efe:EFER_3387; -.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   OrthoDB; 1377603at2; -.
DR   BioCyc; EFER585054:EFER_RS17010-MON; -.
DR   Proteomes; UP000000745; 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_1000139851"
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;  103062 MW;  433AFA3E250BB245 CRC64;
     MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALITSP AGYGKTTLVS QWAAGKSELG
     WFSLDEGDNQ QERFASYLIA AIQQATNGHC TASEVMAQKR QYASLSSLFA QLFIELAEWH
     QPLYLVIDDY HLITNPVIHE SMRFFLRHQP ENLTLVVMSR NLPQLGIANL RVRDQLLEIG
     SQQLAFNHQE AKQFFDRRLT SPIEAAESSR MCDDVSGWAT ALQLIALSAR QNSHSAHQSA
     RRLSGINASH LSDYLVDEVL NNVDLATRHF LLKSAILRSM NDALITRVTG EENGQMRLEE
     IERQGLFLQR MDDSGEWFSY HPLFGNFLRQ RCQWELAAEL PEIHLAAAES WMAQGFPSEA
     IHHALAAGDA SMLRDILLNH AWGLFNHSEL ALLEESLKAL PWESLLENPR LVLLQAWLMQ
     SQHRYSEVNT LLARAEQEIK GEMTGTLHAE FNALRAQVAI NAGNPEEAER LARLALDELP
     IAWFYSRIVA TSVHGEVLHC KGDLSRSLAL MQQTEQMARH HDVWHYALWS LIQQSEIYFA
     QGFLQAAWET QDKAFQLIKE QHLEQLPMHE FLVRIRAQLL WAWSRLDEAE ASARSGIEVL
     SSFQPQQQLQ CLALLVQCSL ARGDLDNART LLNRLENLLG NGQYHSDWIS NADKVRVIYW
     QMTGDKKAAA NWLSQTPKPE FANNHFLQGQ WRNIARAQIL LGEFEPAEIV LEELNENARQ
     LRLMSDLNRN LLLLNQLYWQ AGRKNDAQRV LMEALQLANR TGFISHFVIE GEAMAQQLRQ
     LIQLNTLPEL EQHRAQRILR EINQHHRHKF AHFDENFVER LLNHPEVPEL IRTSPLTQRE
     WQVLGLIYSG YSNEQIAGEL EVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
     V