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 27-MAR-2024, entry version 84.
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; Pseudomonadota; 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 KEGG; kpe:KPK_0326; -.
DR HOGENOM; CLU_006325_3_0_6; -.
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 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_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
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