MALT_KLEP7
ID MALT_KLEP7 Reviewed; 901 AA.
AC A6TF41;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=KPN78578_37510; ORFNames=KPN_03788;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR79175.1; -; Genomic_DNA.
DR RefSeq; WP_015959097.1; NC_009648.1.
DR AlphaFoldDB; A6TF41; -.
DR SMR; A6TF41; -.
DR STRING; 272620.KPN_03788; -.
DR jPOST; A6TF41; -.
DR EnsemblBacteria; ABR79175; ABR79175; KPN_03788.
DR KEGG; kpn:KPN_03788; -.
DR HOGENOM; CLU_006325_3_0_6; -.
DR OMA; SDWVSNA; -.
DR Proteomes; UP000000265; 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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..901
FT /note="HTH-type transcriptional regulator MalT"
FT /id="PRO_1000085773"
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; 103145 MW; DB40C8BB813B066B 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
RRFAGINASH LSDYLVDEVL DNVDARTRNF LLKSSLLRSM NDALIVRVTG EENGQMQLEE
IERQGLFLQR MDDSGEWFRY HPLFGSFLRQ RCQWELAVEL PEIHRAAAES WMAQGFPSEA
IHHALAAGDA KMLRDILLNH AWGMFNHSEL GLLEQSLAAL 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 SGRKSEAQKA LLEALTLANR TGFINHFVIE GEAMAQQLRQ
LIQLNTLPEL EQHRAQRILR DINQHHRHKF AHFDEGFVER LLNHPEVPEL IRTSPLTQRE
WQVLGLIYSG YSNEQIAGEL DVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
V