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Database: UniProt
Entry: B1IP47
LinkDB: B1IP47
Original site: B1IP47 
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   08-MAY-2019, entry version 79.
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=EcolC_0295;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / 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 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., 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
CC       regulon whose gene products are responsible for uptake and
CC       catabolism of malto-oligosaccharides. Specifically binds to the
CC       promoter region of its target genes, recognizing a short DNA motif
CC       called the MalT box. {ECO:0000255|HAMAP-Rule:MF_01247}.
CC   -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are
CC       both required for DNA binding. {ECO:0000255|HAMAP-Rule:MF_01247}.
CC   -!- SUBUNIT: Monomer in solution. Oligomerizes to an active state in
CC       the 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}.
DR   EMBL; CP000946; ACA75973.1; -; Genomic_DNA.
DR   RefSeq; WP_000906956.1; NC_010468.1.
DR   SMR; B1IP47; -.
DR   EnsemblBacteria; ACA75973; ACA75973; EcolC_0295.
DR   KEGG; ecl:EcolC_0295; -.
DR   eggNOG; ENOG41061ZR; Bacteria.
DR   eggNOG; COG2909; LUCA.
DR   HOGENOM; HOG000218261; -.
DR   KO; K03556; -.
DR   OMA; SDWVSNA; -.
DR   BioCyc; ECOL481805:ECOLC_RS01575-MONOMER; -.
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       HTH-type transcriptional regulator MalT.
FT                                /FTId=PRO_1000085769.
FT   DOMAIN      829    894       HTH luxR-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_01247}.
FT   NP_BIND      39     46       ATP. {ECO:0000255|HAMAP-Rule:MF_01247}.
FT   DNA_BIND    853    872       H-T-H motif. {ECO:0000255|HAMAP-
FT                                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
//
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