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 activator mta

Gene

mta

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi5 – 24H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU36600-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional activator mta
Alternative name(s):
Multidrug transporter activation protein
Gene namesi
Name:mta
Synonyms:ywnD
Ordered Locus Names:BSU36600
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003549741 – 257HTH-type transcriptional activator mtaAdd BLAST257

Proteomic databases

PaxDbiP71039.

Expressioni

Inductioni

Autoregulated.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019786.

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 12Combined sources8
Helixi16 – 24Combined sources9
Beta strandi31 – 33Combined sources3
Beta strandi39 – 41Combined sources3
Helixi43 – 57Combined sources15
Helixi62 – 70Combined sources9
Helixi76 – 105Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JBGX-ray2.75A1-109[»]
1R8DX-ray2.70A/B1-109[»]
ProteinModelPortaliP71039.
SMRiP71039.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP71039.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 71HTH merR-typePROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni71 – 74Hinge4
Regioni76 – 104Essential for dimerizationAdd BLAST29

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili76 – 107Add BLAST32

Domaini

The central dimerization domain of the first subunit forms a two-helix antiparallel coiled coil with the dimerization domain of the second subunit.

Sequence similaritiesi

Contains 1 HTH merR-type DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4107TXC. Bacteria.
COG0789. LUCA.
HOGENOMiHOG000240261.
InParanoidiP71039.
OMAiFNTIYRN.
PhylomeDBiP71039.

Family and domain databases

Gene3Di1.10.490.50. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR000551. MerR-type_HTH_dom.
IPR012925. TipAS_dom.
[Graphical view]
PfamiPF13411. MerR_1. 1 hit.
PF07739. TipAS. 1 hit.
[Graphical view]
PRINTSiPR00040. HTHMERR.
SMARTiSM00422. HTH_MERR. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF89082. SSF89082. 1 hit.
PROSITEiPS50937. HTH_MERR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P71039-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYQVKQVAE ISGVSIRTLH HYDNIELLNP SALTDAGYRL YSDADLERLQ
60 70 80 90 100
QILFFKEIGF RLDEIKEMLD HPNFDRKAAL QSQKEILMKK KQRMDEMIQT
110 120 130 140 150
IDRTLLSVDG GETMNKRDLF AGLSMKDIEE HQQTYADEVR KLYGKEIAEE
160 170 180 190 200
TEKRTSAYSA DDWRTIMAEF DSIYRRIAAR MKHGPDDAEI QAAVGAFRDH
210 220 230 240 250
ICQYHYDCTL DIFRGLGEVY ITDERFTDSI NQYGEGLAAF LREAIIIYCD

HQENPRP
Length:257
Mass (Da):29,936
Last modified:February 1, 1997 - v1
Checksum:i98AD46A5CED91DB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08559 Genomic DNA. Translation: CAA69863.1.
AL009126 Genomic DNA. Translation: CAB15677.1.
PIRiC69661.
RefSeqiNP_391541.1. NC_000964.3.
WP_003242936.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15677; CAB15677; BSU36600.
GeneIDi936962.
KEGGibsu:BSU36600.
PATRICi18979348. VBIBacSub10457_3836.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08559 Genomic DNA. Translation: CAA69863.1.
AL009126 Genomic DNA. Translation: CAB15677.1.
PIRiC69661.
RefSeqiNP_391541.1. NC_000964.3.
WP_003242936.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JBGX-ray2.75A1-109[»]
1R8DX-ray2.70A/B1-109[»]
ProteinModelPortaliP71039.
SMRiP71039.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019786.

Proteomic databases

PaxDbiP71039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15677; CAB15677; BSU36600.
GeneIDi936962.
KEGGibsu:BSU36600.
PATRICi18979348. VBIBacSub10457_3836.

Phylogenomic databases

eggNOGiENOG4107TXC. Bacteria.
COG0789. LUCA.
HOGENOMiHOG000240261.
InParanoidiP71039.
OMAiFNTIYRN.
PhylomeDBiP71039.

Enzyme and pathway databases

BioCyciBSUB:BSU36600-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP71039.

Family and domain databases

Gene3Di1.10.490.50. 1 hit.
InterProiIPR009061. DNA-bd_dom_put.
IPR000551. MerR-type_HTH_dom.
IPR012925. TipAS_dom.
[Graphical view]
PfamiPF13411. MerR_1. 1 hit.
PF07739. TipAS. 1 hit.
[Graphical view]
PRINTSiPR00040. HTHMERR.
SMARTiSM00422. HTH_MERR. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF89082. SSF89082. 1 hit.
PROSITEiPS50937. HTH_MERR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTA_BACSU
AccessioniPrimary (citable) accession number: P71039
Secondary accession number(s): Q794Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 114 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.