ID   MALT_KLEP3              Reviewed;         901 AA.
AC   B5XTR7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=KPK_0326;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(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; CP000964; ACI11106.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XTR7; -.
DR   SMR; B5XTR7; -.
DR   EnsemblBacteria; ACI11106; ACI11106; KPK_0326.
DR   KEGG; kpe:KPK_0326; -.
DR   HOGENOM; CLU_006325_3_0_6; -.
DR   OMA; SDWVSNA; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000001734; 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_1000139852"
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;  103111 MW;  77A6B256556D10B0 CRC64;
     MLIPSKLSRP VRLEHTVVRE RLLAKLSGAN NYRLVLITSP AGYGKTTLIS QWAAGKNDLG
     WFSLDEGDNQ QERFASYLIA AIQQATGNHC AASEAMVQKR QYASLSSLFA QLFIELADWQ
     RPLYLVIDDY HLINNPVIHD AMRFFLRHQP ENMTLVVLSR NLPQLGIANL RVRDQLLEIG
     SQQLAFTHQE AKQFFDCRLT SPIEADDSSR LCDDVAGWAT ALQLIALSAR QNNSSAQHSA
     RRLAGINASH LSDYLVDEVL DNVDARTRNF LLKSSLLRSM NDALIVRVTG EENGQMQLEE
     IERQGLFLQR MDDSGEWFRY HPLFGSFLRQ RCQWELAVEL PEIHRAAAES WMAQGFPSEA
     IHHALAAGDA KMLRDILLNH AWGMFNHSEL GLLEQSLSAL PWSNLLENPR LILLQAWLMQ
     SQHRYSEVNT LLARAEQEMS VEMDTAMHGD FNALRAQVAI NDGDQDEAER LSMVALEELP
     LANYYSRIVA TSVHGEVLHC KGKLTKSLAV MQQTEQMARR HDVWHYALWS IIQQSEILFA
     QGFLQAAWES QEKAFQLVRE QHLEQLPMHE FLLRIRSQLL WAWARLDEAE ACARQGMDVL
     STYQPQQQLQ CLALMVQCSL ARGDLDNARS HLNRLENLLG NGHYHSDWVS NADKVRVIYW
     QMTGDKTAAA NWLRQTPKPE FANNHFLQSQ WRNIARAQIL LGDFEPAEMV LEELNENARS
     LRLMSDLNRN LLLLNQLYWQ AGRKSEAQKA LLEALTLANR TGFINHFVIE GEAMAQQLRQ
     LIQLNTLPEL EQHRAQRILR DINQHHRHKF AHFDEGFVER LLNHPEVPEL IRTSPLTQRE
     WQVLGLIYSG YSNEQIAGEL DVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
     V