MALT_ECOLI
ID MALT_ECOLI Reviewed; 901 AA.
AC P06993; Q2M783;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=HTH-type transcriptional regulator MalT {ECO:0000255|HAMAP-Rule:MF_01247, ECO:0000305};
DE AltName: Full=ATP-dependent transcriptional activator MalT {ECO:0000255|HAMAP-Rule:MF_01247, ECO:0000303|PubMed:2524384};
GN Name=malT {ECO:0000255|HAMAP-Rule:MF_01247, ECO:0000303|PubMed:6283313};
GN Synonyms=malA; OrderedLocusNames=b3418, JW3381;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3015733; DOI=10.1016/0378-1119(86)90297-0;
RA Cole S.T., Raibaud O.;
RT "The nucleotide sequence of the malT gene encoding the positive regulator
RT of the Escherichia coli maltose regulon.";
RL Gene 42:201-208(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=6283313; DOI=10.1007/bf00333795;
RA Debarbouille M., Cossart P., Raibaud O.;
RT "A DNA sequence containing the control sites for gene malT and for the
RT malPQ operon.";
RL Mol. Gen. Genet. 185:88-92(1982).
RN [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7040340; DOI=10.1128/jb.150.2.722-729.1982;
RA Chapon C.;
RT "Role of the catabolite activator protein in the maltose regulon of
RT Escherichia coli.";
RL J. Bacteriol. 150:722-729(1982).
RN [6]
RP FUNCTION, ATP-BINDING, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=3305511; DOI=10.1016/s0021-9258(18)45255-6;
RA Richet E., Raibaud O.;
RT "Purification and properties of the MalT protein, the transcription
RT activator of the Escherichia coli maltose regulon.";
RL J. Biol. Chem. 262:12647-12653(1987).
RN [7]
RP FUNCTION, ATP-BINDING, AND ACTIVITY REGULATION.
RX PubMed=2524384; DOI=10.1002/j.1460-2075.1989.tb03461.x;
RA Richer E., Raibaud O.;
RT "MalT, the regulatory protein of the Escherichia coli maltose system, is an
RT ATP-dependent transcriptional activator.";
RL EMBO J. 8:981-987(1989).
RN [8]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2538630; DOI=10.1016/0022-2836(89)90218-0;
RA Raibaud O., Vidal-Ingigliardi D., Richet E.;
RT "A complex nucleoprotein structure involved in activation of transcription
RT of two divergent Escherichia coli promoters.";
RL J. Mol. Biol. 205:471-485(1989).
RN [9]
RP INTERACTION WITH MALK, AND ACTIVITY REGULATION.
RX PubMed=9822819; DOI=10.1046/j.1365-2958.1998.01084.x;
RA Panagiotidis C.H., Boos W., Shuman H.A.;
RT "The ATP-binding cassette subunit of the maltose transporter MalK
RT antagonizes MalT, the activator of the Escherichia coli mal regulon.";
RL Mol. Microbiol. 30:535-546(1998).
RN [10]
RP SUBUNIT.
RX PubMed=10559195; DOI=10.1074/jbc.274.47.33220;
RA Schreiber V., Richet E.;
RT "Self-association of the Escherichia coli transcription activator MalT in
RT the presence of maltotriose and ATP.";
RL J. Biol. Chem. 274:33220-33226(1999).
RN [11]
RP INTERACTION WITH MALY, AND ACTIVITY REGULATION.
RX PubMed=10692154; DOI=10.1046/j.1365-2958.2000.01747.x;
RA Schreiber V., Steegborn C., Clausen T., Boos W., Richet E.;
RT "A new mechanism for the control of a prokaryotic transcriptional
RT regulator: antagonistic binding of positive and negative effectors.";
RL Mol. Microbiol. 35:765-776(2000).
RN [12]
RP DOMAINS OF INTERACTION WITH REPRESSORS.
RX PubMed=12003949; DOI=10.1128/jb.184.11.3069-3077.2002;
RA Schlegel A., Danot O., Richet E., Ferenci T., Boos W.;
RT "The N-terminus of the Escherichia coli transcription activator MalT is the
RT domain of interaction with MalY.";
RL J. Bacteriol. 184:3069-3077(2002).
RN [13]
RP INTERACTION WITH AES, AND ACTIVITY REGULATION.
RX PubMed=11867639; DOI=10.1074/jbc.m200991200;
RA Joly N., Danot O., Schlegel A., Boos W., Richet E.;
RT "The Aes protein directly controls the activity of MalT, the central
RT transcriptional activator of the Escherichia coli maltose regulon.";
RL J. Biol. Chem. 277:16606-16613(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 437-806, AND DOMAIN.
RX PubMed=11709169; DOI=10.1016/s0969-2126(01)00665-7;
RA Steegborn C., Danot O., Huber R., Clausen T.;
RT "Crystal structure of transcription factor MalT domain III: a novel helix
RT repeat fold implicated in regulated oligomerization.";
RL Structure 9:1051-1060(2001).
CC -!- FUNCTION: Positively regulates the transcription of the maltose regulon
CC whose gene products are responsible for uptake and catabolism of malto-
CC oligosaccharides (PubMed:7040340, PubMed:3305511, PubMed:2538630,
CC PubMed:2524384). Specifically binds to the promoter region of its
CC target genes, recognizing a short DNA motif called the MalT box (5'-
CC GGA[TG]GA-3') (PubMed:2538630, PubMed:2524384). Displays weak ATPase
CC activity, but this activity is not required for promoter binding
CC (PubMed:2524384). {ECO:0000269|PubMed:2524384,
CC ECO:0000269|PubMed:2538630, ECO:0000269|PubMed:3305511,
CC ECO:0000269|PubMed:7040340}.
CC -!- ACTIVITY REGULATION: Activated by ATP and maltotriose, which are both
CC required for DNA binding (PubMed:3305511, PubMed:2524384). Negatively
CC regulated by MalY, MalK and Aes, which bind to MalT and block
CC maltotriose activation (PubMed:9822819, PubMed:10692154,
CC PubMed:11867639). {ECO:0000269|PubMed:10692154,
CC ECO:0000269|PubMed:11867639, ECO:0000269|PubMed:2524384,
CC ECO:0000269|PubMed:3305511, ECO:0000269|PubMed:9822819}.
CC -!- SUBUNIT: Monomer in solution (PubMed:3305511, PubMed:10559195).
CC Oligomerizes to an active state in the presence of the positive
CC effectors ATP and maltotriose (PubMed:10559195). Interacts with MalY,
CC MalK and Aes, all of which negatively regulate MalT activity by
CC antagonizing maltotriose binding (PubMed:9822819, PubMed:10692154,
CC PubMed:11867639). {ECO:0000269|PubMed:10559195,
CC ECO:0000269|PubMed:10692154, ECO:0000269|PubMed:11867639,
CC ECO:0000269|PubMed:3305511, ECO:0000269|PubMed:9822819}.
CC -!- INTERACTION:
CC P06993; P08622: dnaJ; NbExp=5; IntAct=EBI-542934, EBI-545285;
CC P06993; P31574: fixB; NbExp=3; IntAct=EBI-542934, EBI-554030;
CC P06993; P52613: fliJ; NbExp=3; IntAct=EBI-542934, EBI-554036;
CC P06993; P0ACG8: hslR; NbExp=2; IntAct=EBI-542934, EBI-562824;
CC P06993; P06993: malT; NbExp=3; IntAct=EBI-542934, EBI-542934;
CC P06993; P36979: rlmN; NbExp=3; IntAct=EBI-542934, EBI-559071;
CC -!- INDUCTION: Expression is induced by the cAMP-activated global
CC transcriptional regulator CRP. {ECO:0000269|PubMed:7040340}.
CC -!- DOMAIN: Consists of four structural domains: the ATP binding site
CC resides in domain I (DT1); DT3 binds the positive effector maltotriose
CC with a low affinity, and the binding affinity is increased in the
CC presence of DT2; the C-terminal domain DT4 contains the helix-turn-
CC helix DNA binding motif. DT1 also contains the region that interacts
CC with MalY (but not with MalK), and the binding site for Aes is also
CC likely to be contained in the N-terminal portion of MalT encompassing
CC DT1 and DT2 (PubMed:12003949). Domain DT3 may mediate oligomerization
CC (PubMed:11709169). {ECO:0000269|PubMed:11709169,
CC ECO:0000269|PubMed:12003949}.
CC -!- MISCELLANEOUS: A study on malT mutants has shown that some of them
CC became nearly completely resistant to Aes repression while still being
CC sensitive to MalY. These mutations are located at positions 38, 220,
CC 243, and 359, most likely defining the interaction patch with Aes on
CC the three-dimensional structure of MalT. {ECO:0000305|PubMed:12003949}.
CC -!- SIMILARITY: Belongs to the MalT family. {ECO:0000255|HAMAP-
CC Rule:MF_01247, ECO:0000305}.
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DR EMBL; M13585; AAA83888.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58216.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U00096; AAC76443.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77873.1; -; Genomic_DNA.
DR EMBL; M24342; AAA24107.2; -; Genomic_DNA.
DR EMBL; V00304; CAA23583.1; -; Genomic_DNA.
DR EMBL; X02003; CAA26034.1; -; Genomic_DNA.
DR PIR; E65137; RGECMT.
DR RefSeq; NP_417877.1; NC_000913.3.
DR RefSeq; WP_000906961.1; NZ_SSZK01000008.1.
DR PDB; 1HZ4; X-ray; 1.45 A; A=437-806.
DR PDBsum; 1HZ4; -.
DR AlphaFoldDB; P06993; -.
DR SMR; P06993; -.
DR BioGRID; 4261189; 24.
DR BioGRID; 852230; 16.
DR DIP; DIP-10149N; -.
DR IntAct; P06993; 30.
DR STRING; 511145.b3418; -.
DR jPOST; P06993; -.
DR PaxDb; P06993; -.
DR PRIDE; P06993; -.
DR EnsemblBacteria; AAC76443; AAC76443; b3418.
DR EnsemblBacteria; BAE77873; BAE77873; BAE77873.
DR GeneID; 947921; -.
DR KEGG; ecj:JW3381; -.
DR KEGG; eco:b3418; -.
DR PATRIC; fig|1411691.4.peg.3310; -.
DR EchoBASE; EB0557; -.
DR eggNOG; COG2909; Bacteria.
DR HOGENOM; CLU_006325_3_0_6; -.
DR InParanoid; P06993; -.
DR OMA; SDWVSNA; -.
DR PhylomeDB; P06993; -.
DR BioCyc; EcoCyc:PD00237; -.
DR BioCyc; MetaCyc:PD00237; -.
DR EvolutionaryTrace; P06993; -.
DR PRO; PR:P06993; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048031; F:trisaccharide binding; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000184163"
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 REGION 1..241
FT /note="DT1"
FT /evidence="ECO:0000305|PubMed:12003949"
FT REGION 242..436
FT /note="DT2"
FT /evidence="ECO:0000305|PubMed:12003949"
FT REGION 437..806
FT /note="DT3"
FT /evidence="ECO:0000305|PubMed:11709169,
FT ECO:0000305|PubMed:12003949"
FT REGION 807..901
FT /note="DT4"
FT /evidence="ECO:0000305|PubMed:12003949"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01247"
FT CONFLICT 192..193
FT /note="KQ -> NE (in Ref. 1; AAA83888/AAA58216)"
FT /evidence="ECO:0000305"
FT HELIX 442..461
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 484..501
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 504..520
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 524..540
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 544..560
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 568..582
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 586..599
FT /evidence="ECO:0007829|PDB:1HZ4"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 605..608
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 609..622
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 625..639
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 646..662
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 666..675
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 688..700
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 704..720
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 724..741
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 744..761
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 765..768
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 771..783
FT /evidence="ECO:0007829|PDB:1HZ4"
FT HELIX 789..802
FT /evidence="ECO:0007829|PDB:1HZ4"
SQ SEQUENCE 901 AA; 103118 MW; 9B27CE0F632AD417 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 ASARSGIEVL
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
