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Protein

HTH-type transcriptional regulator MalT

Gene

malT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides. Binds and recognizes a DNA motif (called the malT box): 5'-GGA[TG]GA-3'.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 468ATPSequence analysis
DNA bindingi853 – 87220H-T-H motifSequence analysisAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • DNA binding Source: UniProtKB-HAMAP
  • identical protein binding Source: IntAct
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB-HAMAP
  • trisaccharide binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Carbohydrate metabolism, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00237.
ECOL316407:JW3381-MONOMER.
MetaCyc:PD00237.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator MalT
Alternative name(s):
ATP-dependent transcriptional activator MalT
Gene namesi
Name:malT
Synonyms:malA
Ordered Locus Names:b3418, JW3381
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10562. malT.

Pathology & Biotechi

Chemistry

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 901901HTH-type transcriptional regulator MalTPRO_0000184163Add
BLAST

Proteomic databases

PaxDbiP06993.
PRIDEiP06993.

Interactioni

Subunit structurei

Monomer in solution but oligomerizes to an active state in the presence of the positive effectors ATP and maltotriose. Interacts with MalY, MalK and Aes, all of which negatively regulate MalT activity by antagonizing maltotriose binding.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-542934,EBI-542934
dnaJP086223EBI-542934,EBI-545285
hslRP0ACG82EBI-542934,EBI-562824

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261189. 19 interactions.
852230. 1 interaction.
DIPiDIP-10149N.
IntActiP06993. 29 interactions.
MINTiMINT-1233939.
STRINGi511145.b3418.

Structurei

Secondary structure

1
901
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi442 – 46120Combined sources
Helixi465 – 47713Combined sources
Helixi484 – 50118Combined sources
Helixi504 – 52017Combined sources
Helixi524 – 54017Combined sources
Helixi544 – 56017Combined sources
Helixi568 – 58215Combined sources
Helixi586 – 59914Combined sources
Turni600 – 6023Combined sources
Helixi605 – 6084Combined sources
Helixi609 – 62214Combined sources
Helixi625 – 63915Combined sources
Helixi646 – 66217Combined sources
Helixi666 – 67510Combined sources
Helixi685 – 6873Combined sources
Helixi688 – 70013Combined sources
Helixi704 – 72017Combined sources
Helixi724 – 74118Combined sources
Helixi744 – 76118Combined sources
Helixi765 – 7684Combined sources
Helixi771 – 78313Combined sources
Helixi789 – 80214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZ4X-ray1.45A437-806[»]
ProteinModelPortaliP06993.
SMRiP06993. Positions 438-803, 836-892.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06993.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini829 – 89466HTH luxR-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 241241DT1Add
BLAST
Regioni242 – 436195DT2Add
BLAST
Regioni437 – 806370DT3Add
BLAST

Domaini

Consists of four structural domains: the ATP binding site resides in domain I (DT1); DT3 binds the positive effector maltotriose with a low affinity, and the binding affinity is increased in the presence of DT2; the C-terminal domain DT4 contains the helix-turn-helix DNA binding motif. DT1 also contains the region that interacts with MalY (but not with MalK), and the binding site for aes is also likely to be contained in the N-terminal portion of MalT encompassing DT1 and DT2.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41061ZR. Bacteria.
COG2909. LUCA.
HOGENOMiHOG000218261.
InParanoidiP06993.
KOiK03556.
OMAiSDWVSNA.
OrthoDBiEOG69GZGV.
PhylomeDBiP06993.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01247. HTH_type_MalT.
InterProiIPR027417. P-loop_NTPase.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR011990. TPR-like_helical_dom.
IPR023768. Tscrpt_reg_HTH_MalT.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF48452. SSF48452. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00622. HTH_LUXR_1. 1 hit.
PS50043. HTH_LUXR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06993-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALITSP AGYGKTTLIS
60 70 80 90 100
QWAAGKNDIG WYSLDEGDNQ QERFASYLIA AVQQATNGHC AICETMAQKR
110 120 130 140 150
QYASLTSLFA QLFIELAEWH SPLYLVIDDY HLITNPVIHE SMRFFIRHQP
160 170 180 190 200
ENLTLVVLSR NLPQLGIANL RVRDQLLEIG SQQLAFTHQE AKQFFDCRLS
210 220 230 240 250
SPIEAAESSR ICDDVSGWAT ALQLIALSAR QNTHSAHKSA RRLAGINASH
260 270 280 290 300
LSDYLVDEVL DNVDLATRHF LLKSAILRSM NDALITRVTG EENGQMRLEE
310 320 330 340 350
IERQGLFLQR MDDTGEWFCY HPLFGNFLRQ RCQWELAAEL PEIHRAAAES
360 370 380 390 400
WMAQGFPSEA IHHALAAGDA LMLRDILLNH AWSLFNHSEL SLLEESLKAL
410 420 430 440 450
PWDSLLENPQ LVLLQAWLMQ SQHRYGEVNT LLARAEHEIK DIREDTMHAE
460 470 480 490 500
FNALRAQVAI NDGNPDEAER LAKLALEELP PGWFYSRIVA TSVLGEVLHC
510 520 530 540 550
KGELTRSLAL MQQTEQMARQ HDVWHYALWS LIQQSEILFA QGFLQTAWET
560 570 580 590 600
QEKAFQLINE QHLEQLPMHE FLVRIRAQLL WAWARLDEAE ASARSGIEVL
610 620 630 640 650
SSYQPQQQLQ CLAMLIQCSL ARGDLDNARS QLNRLENLLG NGKYHSDWIS
660 670 680 690 700
NANKVRVIYW QMTGDKAAAA NWLRHTAKPE FANNHFLQGQ WRNIARAQIL
710 720 730 740 750
LGEFEPAEIV LEELNENARS LRLMSDLNRN LLLLNQLYWQ AGRKSDAQRV
760 770 780 790 800
LLDALKLANR TGFISHFVIE GEAMAQQLRQ LIQLNTLPEL EQHRAQRILR
810 820 830 840 850
EINQHHRHKF AHFDENFVER LLNHPEVPEL IRTSPLTQRE WQVLGLIYSG
860 870 880 890 900
YSNEQIAGEL EVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG

V
Length:901
Mass (Da):103,118
Last modified:July 19, 2003 - v2
Checksum:i9B27CE0F632AD417
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1932KQ → NE in AAA83888 (PubMed:3015733).Curated
Sequence conflicti192 – 1932KQ → NE in AAA58216 (PubMed:3015733).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13585 Genomic DNA. Translation: AAA83888.1.
U18997 Genomic DNA. Translation: AAA58216.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC76443.1.
AP009048 Genomic DNA. Translation: BAE77873.1.
M24342 Genomic DNA. Translation: AAA24107.2.
V00304 Genomic DNA. Translation: CAA23583.1.
X02003 Genomic DNA. Translation: CAA26034.1.
PIRiE65137. RGECMT.
RefSeqiNP_417877.1. NC_000913.3.
WP_000906961.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC76443; AAC76443; b3418.
BAE77873; BAE77873; BAE77873.
GeneIDi947921.
KEGGiecj:JW3381.
eco:b3418.
PATRICi32122274. VBIEscCol129921_3514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13585 Genomic DNA. Translation: AAA83888.1.
U18997 Genomic DNA. Translation: AAA58216.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC76443.1.
AP009048 Genomic DNA. Translation: BAE77873.1.
M24342 Genomic DNA. Translation: AAA24107.2.
V00304 Genomic DNA. Translation: CAA23583.1.
X02003 Genomic DNA. Translation: CAA26034.1.
PIRiE65137. RGECMT.
RefSeqiNP_417877.1. NC_000913.3.
WP_000906961.1. NZ_CP014272.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZ4X-ray1.45A437-806[»]
ProteinModelPortaliP06993.
SMRiP06993. Positions 438-803, 836-892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261189. 19 interactions.
852230. 1 interaction.
DIPiDIP-10149N.
IntActiP06993. 29 interactions.
MINTiMINT-1233939.
STRINGi511145.b3418.

Chemistry

DrugBankiDB03793. Benzoic Acid.

Proteomic databases

PaxDbiP06993.
PRIDEiP06993.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76443; AAC76443; b3418.
BAE77873; BAE77873; BAE77873.
GeneIDi947921.
KEGGiecj:JW3381.
eco:b3418.
PATRICi32122274. VBIEscCol129921_3514.

Organism-specific databases

EchoBASEiEB0557.
EcoGeneiEG10562. malT.

Phylogenomic databases

eggNOGiENOG41061ZR. Bacteria.
COG2909. LUCA.
HOGENOMiHOG000218261.
InParanoidiP06993.
KOiK03556.
OMAiSDWVSNA.
OrthoDBiEOG69GZGV.
PhylomeDBiP06993.

Enzyme and pathway databases

BioCyciEcoCyc:PD00237.
ECOL316407:JW3381-MONOMER.
MetaCyc:PD00237.

Miscellaneous databases

EvolutionaryTraceiP06993.
PROiP06993.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01247. HTH_type_MalT.
InterProiIPR027417. P-loop_NTPase.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR011990. TPR-like_helical_dom.
IPR023768. Tscrpt_reg_HTH_MalT.
IPR000792. Tscrpt_reg_LuxR_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00196. GerE. 1 hit.
[Graphical view]
PRINTSiPR00038. HTHLUXR.
SMARTiSM00421. HTH_LUXR. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF48452. SSF48452. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00622. HTH_LUXR_1. 1 hit.
PS50043. HTH_LUXR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon."
    Cole S.T., Raibaud O.
    Gene 42:201-208(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "A DNA sequence containing the control sites for gene malT and for the malPQ operon."
    Debarbouille M., Cossart P., Raibaud O.
    Mol. Gen. Genet. 185:88-92(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
  5. "MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator."
    Richer E., Raibaud O.
    EMBO J. 8:981-987(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: ATP-BINDING.
  6. "The N-terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY."
    Schlegel A., Danot O., Richet E., Ferenci T., Boos W.
    J. Bacteriol. 184:3069-3077(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS OF INTERACTION WITH REPRESSORS.
  7. "Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization."
    Steegborn C., Danot O., Huber R., Clausen T.
    Structure 9:1051-1060(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 437-806.

Entry informationi

Entry nameiMALT_ECOLI
AccessioniPrimary (citable) accession number: P06993
Secondary accession number(s): Q2M783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 19, 2003
Last modified: May 11, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

A study on malT mutants (PubMed:12003949) has shown that some of them became nearly completely resistant to Aes repression while still being sensitive to MalY. These mutations are located at positions 38, 220, 243, and 359, most likely defining the interaction patch with aes on the three-dimensional structure of MalT.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.