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Protein

HTH-type transcriptional repressor AseR

Gene

aseR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Metal-responsive transcriptional regulator that represses transcription of the aseR-ydfA operon by binding specifically to its promoter. Binding of arsenite or antimonite causes the repressor to dissociate from the DNA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi33 – 331ArsenitePROSITE-ProRule annotation
Metal bindingi35 – 351ArsenitePROSITE-ProRule annotation
Metal bindingi39 – 391ArsenitePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi34 – 5724H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Metal-thiolate cluster

Enzyme and pathway databases

BioCyciBSUB:BSU05330-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional repressor AseR
Gene namesi
Name:aseR
Synonyms:ydeT
Ordered Locus Names:BSU05330
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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331C → S: Binds DNA, but loss of arsenite-mediated regulation; when associated with S-35. 1 Publication
Mutagenesisi35 – 351C → S: Binds DNA, but loss of arsenite-mediated regulation; when associated with S-33. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111HTH-type transcriptional repressor AseRPRO_0000378471Add
BLAST

Proteomic databases

PaxDbiP96677.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002998.

Structurei

3D structure databases

ProteinModelPortaliP96677.
SMRiP96677. Positions 8-94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 105105HTH arsR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41082YX. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
InParanoidiP96677.
KOiK03892.
OMAiCQLVDMF.
OrthoDBiEOG6W9X9K.
PhylomeDBiP96677.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSiPR00778. HTHARSR.
SMARTiSM00418. HTH_ARSR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50987. HTH_ARSR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P96677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIDVAAMTR CLKTLSDQTR LIMMRLFLEQ EYCVCQLVDM FEMSQPAISQ
60 70 80 90 100
HLRKLKNAGF VNEDRRGQWR YYSINGSCPE FDTLQLILHQ IDQEDELLNH
110
IKQKKTQACC Q
Length:111
Mass (Da):13,088
Last modified:May 1, 1997 - v1
Checksum:i3E2B4088061AB1A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19367.1.
AL009126 Genomic DNA. Translation: CAB12340.1.
PIRiF69779.
RefSeqiNP_388414.1. NC_000964.3.
WP_003243257.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12340; CAB12340; BSU05330.
GeneIDi938089.
KEGGibsu:BSU05330.
PATRICi18972668. VBIBacSub10457_0555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001488 Genomic DNA. Translation: BAA19367.1.
AL009126 Genomic DNA. Translation: CAB12340.1.
PIRiF69779.
RefSeqiNP_388414.1. NC_000964.3.
WP_003243257.1. NZ_JNCM01000031.1.

3D structure databases

ProteinModelPortaliP96677.
SMRiP96677. Positions 8-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100002998.

Proteomic databases

PaxDbiP96677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12340; CAB12340; BSU05330.
GeneIDi938089.
KEGGibsu:BSU05330.
PATRICi18972668. VBIBacSub10457_0555.

Phylogenomic databases

eggNOGiENOG41082YX. Bacteria.
COG0640. LUCA.
HOGENOMiHOG000144506.
InParanoidiP96677.
KOiK03892.
OMAiCQLVDMF.
OrthoDBiEOG6W9X9K.
PhylomeDBiP96677.

Enzyme and pathway databases

BioCyciBSUB:BSU05330-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001845. HTH_ArsR_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01022. HTH_5. 1 hit.
[Graphical view]
PRINTSiPR00778. HTHARSR.
SMARTiSM00418. HTH_ARSR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50987. HTH_ARSR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus subtilis genome."
    Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Predicting metals sensed by ArsR-SmtB repressors: allosteric interference by a non-effector metal."
    Harvie D.R., Andreini C., Cavallaro G., Meng W., Connolly B.A., Yoshida K., Fujita Y., Harwood C.R., Radford D.S., Tottey S., Cavet J.S., Robinson N.J.
    Mol. Microbiol. 59:1341-1356(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF CYS-33 AND CYS-35.
    Strain: 168.

Entry informationi

Entry nameiASER_BACSU
AccessioniPrimary (citable) accession number: P96677
Secondary accession number(s): Q797H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: May 1, 1997
Last modified: February 17, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Can also bind zinc in vitro, but it does not impair DNA binding.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. 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.