Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

HTH-type transcriptional regulator MalT

Gene

malT

Organism
Escherichia coli O1:K1 / APEC
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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'.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 468ATPUniRule annotation
DNA bindingi853 – 87220H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator MalTUniRule annotation
Alternative name(s):
ATP-dependent transcriptional activator MalTUniRule annotation
Gene namesi
Name:malTUniRule annotation
Ordered Locus Names:Ecok1_33880
ORF Names:APECO1_3048
OrganismiEscherichia coli O1:K1 / APEC
Taxonomic identifieri405955 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000008216 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 901901HTH-type transcriptional regulator MalTPRO_1000085767Add
BLAST

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA1AGU2.
SMRiA1AGU2. Positions 438-803, 832-892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 HTH luxR-type DNA-binding domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000218261.
KOiK03556.
OMAiSDWVSNA.

Family and domain databases

CDDicd06170. LuxR_C_like. 1 hit.
Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01247. HTH_type_MalT. 1 hit.
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.

A1AGU2-1 [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 DIREGTMHAE
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
LGEFESAEIV 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 AHRQAAVQHA QKLLKMMGYG

V
Length:901
Mass (Da):103,006
Last modified:January 23, 2007 - v1
Checksum:i4E5F1E3F3FA6FA54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABJ02882.1.
RefSeqiWP_000906972.1. NC_008563.1.

Genome annotation databases

EnsemblBacteriaiABJ02882; ABJ02882; APECO1_3048.
KEGGiecv:APECO1_3048.
PATRICi18219213. VBIEscCol127180_3834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABJ02882.1.
RefSeqiWP_000906972.1. NC_008563.1.

3D structure databases

ProteinModelPortaliA1AGU2.
SMRiA1AGU2. Positions 438-803, 832-892.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ02882; ABJ02882; APECO1_3048.
KEGGiecv:APECO1_3048.
PATRICi18219213. VBIEscCol127180_3834.

Phylogenomic databases

HOGENOMiHOG000218261.
KOiK03556.
OMAiSDWVSNA.

Family and domain databases

CDDicd06170. LuxR_C_like. 1 hit.
Gene3Di1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01247. HTH_type_MalT. 1 hit.
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...

Entry informationi

Entry nameiMALT_ECOK1
AccessioniPrimary (citable) accession number: A1AGU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.