MALT_ECOLC
ID MALT_ECOLC Reviewed; 901 AA.
AC B1IP47;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=EcolC_0295;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) 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; CP000946; ACA75973.1; -; Genomic_DNA.
DR RefSeq; WP_000906956.1; NC_010468.1.
DR AlphaFoldDB; B1IP47; -.
DR SMR; B1IP47; -.
DR KEGG; ecl:EcolC_0295; -.
DR HOGENOM; CLU_006325_3_0_6; -.
DR OMA; SDWVSNA; -.
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_1000085769"
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; 103188 MW; 3B277EC808471560 CRC64;
MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALITSP AGYGKTTLIS QWAAGKNDIG
WYSLDEGDNQ QERFASYLIA AVQQATNGHC AICETMAQKR QYASLTSLFA QLFIELAEWH
SPLYLVIDDY HLITNPVIHE SMRFFIRHQP ENLTLVVLSR NLPQLGIANL RVRDQLLEIG
SQQLAFTHQE AKQFFDCRLS SPIEAAESSR ICDDVSGWAT ALQLIALSAR QNTHSAHKSA
RRLAGINASH LSDYLVDEVL DNVDLATRHF LLKSAILRSM NDALITRVTG EENGQMRLEE
IERQGLFLQR MDDTGEWFCY HPLFGNFLRQ RCQWELAAEL PEIHRAAAES WMAQGFPSEA
IHHALAAGDA LMLRDILLNH AWSLFNHSEL SLLEESLKAL PWDSLLENPQ LVLLQAWLMQ
SQHRYGEVNT LLARAEHEIK DIREDTMHAE FNALRAQVAI NDGNPDEAER LAKLALEELP
PGWFYSRIVA TSVLGEVLHC KGELTRSLAL MQQTEQMARQ HDVWHYALWS LIQQSEILFA
QGFLQTAWET QEKAFQLINE QHLEQLPMHE FLVRIRAQLL WAWARLDEAE ASARRGIEVL
SSYQPQQQLQ CLAMLIQCSL ARGDLDNARS QLNRLENLLG NGKYHSDWIS NANKVRVIYW
QMTGDKAAAA NWLRHTAKPE FANNHFLQGQ WRNIARAQIL LGEFEPAEIV LEELNENARS
LRLMSDLNRN LLLLNQLYWQ AGRKSDAQRV LLDALKLANR TGFISHFVIE GEAMAQQLRQ
LIQLNTLPEL EQHRAQRILR EINQHHRHKF AHFDENFVER LLNHPEVPEL IRTSPLTQRE
WQVLGLIYSG YSNEQIAGEL EVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
V