ID   MALT_CROS8              Reviewed;         901 AA.
AC   A7ME76;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=ESA_04320;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(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; CP000783; ABU79499.1; -; Genomic_DNA.
DR   RefSeq; WP_012126376.1; NC_009778.1.
DR   AlphaFoldDB; A7ME76; -.
DR   SMR; A7ME76; -.
DR   EnsemblBacteria; ABU79499; ABU79499; ESA_04320.
DR   KEGG; esa:ESA_04320; -.
DR   PATRIC; fig|290339.8.peg.3847; -.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000000260; 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..901
FT                   /note="HTH-type transcriptional regulator MalT"
FT                   /id="PRO_1000085772"
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;  102610 MW;  9BDC56FBE85985D4 CRC64;
     MLIPSKLSRP VRLEHTVVRE RLLAKLSGAS NYRLALITSP AGYGKTTLIS QWAAGKTELG
     WYSLDEGDNQ PERFASYLIA AIQQATGGHC ASSEVMAQKR QYASLSSLFA QLFIELAAWP
     RPLFLVIDDY HLITNPVIHE AMRFFLRHQP DHLTLVVLSR NLPQLGIANL RVREQLLEIG
     SQQLAFTHQE ARQFFDCRLS QPIEPAQSNR LCDDVAGWAT ALQLIALSAR QNTGAVHQSA
     RRLAGINASH LSDYLVDEVL NNVDNDTRQF LLKSALLRSM NDALIARVTG EENGQMRLEE
     IERQGLFLQR MDDSGEWFSY HPLFGSFLRQ RCQWELSTEL PDIHRAAAES WMAQGFPSEA
     IHHALAAGDA SMLRDILLNH AWGLFNHSEL TLLEQSLKAL PWESLLANPR LVLLQAWLMQ
     SQHRYSEVNT LLARAEQEMK GEMDDTLHGE FNALRAQVAI NDGDPDEAER LAMVALETLP
     LANFYSRIVA TSVHGEVLHC KGDLTKSLSV MQQTELMARR HDVWHYALWS LIQQSEILFA
     QGFLQAAWET QEKAFTLIQE QHLEQLPLHE FLLRIRAQLL WAWARLDEAE ACARTGMTVL
     ANYQPQQQLQ CLALLVQCSL ARGDLDNARS HLNRLENLLG NGHYHSDWVS NADKVRVIYW
     QMTGDKAAAA AWLRQTPKPA FANNHFLQSQ WRNIARVQIL LGDYEPAEMV LEELNENARS
     LRLMSDINRN LLLLNQLYWN AGRKSDAQRV LMEALTLANR TGFISHFVIE GEAMAQQLRQ
     LLQLNTLPEI EQHRAQRILR DINQHHRHKF AHFDENFVNK LLNHPEVPEL IRTSPLTQRE
     WQVLGLIYSG YSNDQIAGEL DVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
     V