Skip Header

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

P0A6R3

- FIS_ECOLI

UniProt

P0A6R3 - FIS_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA-binding protein Fis

Gene

fis

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin-mediated DNA inversion. Prevents initiation of DNA replication from oriC.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi74 – 9320H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: EcoCyc
  2. sequence-specific DNA binding Source: EcoliWiki
  3. sequence-specific DNA binding transcription factor activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: EcoCyc
  2. regulation of transcription by chromatin organization Source: EcoCyc
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00196.
ECOL316407:JW3229-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein FisUniRule annotation
Alternative name(s):
Factor-for-inversion stimulation protein
Hin recombinational enhancer-binding protein
Gene namesi
Name:fisUniRule annotation
Ordered Locus Names:b3261, JW3229
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10317. fis.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic nucleosome Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9898DNA-binding protein FisPRO_0000203878Add
BLAST

Proteomic databases

PaxDbiP0A6R3.
PRIDEiP0A6R3.

Expressioni

Gene expression databases

GenevestigatoriP0A6R3.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
yebVP645033EBI-550170,EBI-9126792

Protein-protein interaction databases

DIPiDIP-47975N.
IntActiP0A6R3. 25 interactions.
MINTiMINT-1225073.
STRINGi511145.b3261.

Structurei

Secondary structure

1
98
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154
Turni18 – 203
Beta strandi23 – 264
Helixi27 – 4216
Helixi50 – 6920
Turni70 – 723
Helixi74 – 818
Helixi85 – 9410

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ETKX-ray2.10A/B1-98[»]
1ETOX-ray1.90A/B1-98[»]
1ETQX-ray2.80A/B/C/D1-98[»]
1ETVX-ray2.00A/B1-98[»]
1ETWX-ray2.00A/B1-98[»]
1ETXX-ray1.90A/B1-98[»]
1ETYX-ray2.00A/B1-98[»]
1F36X-ray2.65A/B1-98[»]
1FIAX-ray2.00A/B1-98[»]
1FIPX-ray1.90A/B1-98[»]
3FISX-ray2.30A/B1-98[»]
3IV5X-ray2.90A/B1-98[»]
3JR9X-ray2.90A/B1-98[»]
3JRAX-ray3.11A/B1-98[»]
3JRBX-ray3.10A/B1-98[»]
3JRCX-ray3.08A/B1-98[»]
3JRDX-ray3.10A/B1-98[»]
3JREX-ray3.17A/B1-98[»]
3JRFX-ray3.05A/B1-98[»]
3JRGX-ray3.11A/B1-98[»]
3JRHX-ray2.88A/B1-98[»]
3JRIX-ray3.11A/B1-98[»]
4FISX-ray2.30A/B1-98[»]
DisProtiDP00422.
ProteinModelPortaliP0A6R3.
SMRiP0A6R3. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6R3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 4428Required for the stimulation of HIN-mediated recombinationAdd
BLAST

Sequence similaritiesi

Belongs to the transcriptional regulatory Fis family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2901.
HOGENOMiHOG000256331.
InParanoidiP0A6R3.
KOiK03557.
OMAiHNQTRAA.
OrthoDBiEOG67HJXZ.
PhylomeDBiP0A6R3.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
HAMAPiMF_00166. DNA_binding_Fis.
InterProiIPR005412. Fis_DNA-bd.
IPR009057. Homeodomain-like.
IPR002197. HTH_Fis.
[Graphical view]
PfamiPF02954. HTH_8. 1 hit.
[Graphical view]
PIRSFiPIRSF002097. DNA-binding_Fis. 1 hit.
PRINTSiPR01591. DNABINDNGFIS.
PR01590. HTHFIS.
SUPFAMiSSF46689. SSF46689. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6R3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFEQRVNSDV LTVSTVNSQD QVTQKPLRDS VKQALKNYFA QLNGQDVNDL
60 70 80 90
YELVLAEVEQ PLLDMVMQYT RGNQTRAALM MGINRGTLRK KLKKYGMN
Length:98
Mass (Da):11,240
Last modified:May 10, 2005 - v1
Checksum:i2E339BFCFCDB163C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03245 Genomic DNA. Translation: AAA83856.1.
J03816 Genomic DNA. Translation: AAA98812.1.
M95784 Genomic DNA. Translation: AAA23783.1.
U18997 Genomic DNA. Translation: AAA58065.1.
U00096 Genomic DNA. Translation: AAC76293.1.
AP009048 Genomic DNA. Translation: BAE77302.1.
PIRiA32142. DNECFS.
RefSeqiNP_417727.1. NC_000913.3.
YP_491443.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76293; AAC76293; b3261.
BAE77302; BAE77302; BAE77302.
GeneIDi12932870.
947697.
KEGGiecj:Y75_p3179.
eco:b3261.
PATRICi32121952. VBIEscCol129921_3360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03245 Genomic DNA. Translation: AAA83856.1 .
J03816 Genomic DNA. Translation: AAA98812.1 .
M95784 Genomic DNA. Translation: AAA23783.1 .
U18997 Genomic DNA. Translation: AAA58065.1 .
U00096 Genomic DNA. Translation: AAC76293.1 .
AP009048 Genomic DNA. Translation: BAE77302.1 .
PIRi A32142. DNECFS.
RefSeqi NP_417727.1. NC_000913.3.
YP_491443.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ETK X-ray 2.10 A/B 1-98 [» ]
1ETO X-ray 1.90 A/B 1-98 [» ]
1ETQ X-ray 2.80 A/B/C/D 1-98 [» ]
1ETV X-ray 2.00 A/B 1-98 [» ]
1ETW X-ray 2.00 A/B 1-98 [» ]
1ETX X-ray 1.90 A/B 1-98 [» ]
1ETY X-ray 2.00 A/B 1-98 [» ]
1F36 X-ray 2.65 A/B 1-98 [» ]
1FIA X-ray 2.00 A/B 1-98 [» ]
1FIP X-ray 1.90 A/B 1-98 [» ]
3FIS X-ray 2.30 A/B 1-98 [» ]
3IV5 X-ray 2.90 A/B 1-98 [» ]
3JR9 X-ray 2.90 A/B 1-98 [» ]
3JRA X-ray 3.11 A/B 1-98 [» ]
3JRB X-ray 3.10 A/B 1-98 [» ]
3JRC X-ray 3.08 A/B 1-98 [» ]
3JRD X-ray 3.10 A/B 1-98 [» ]
3JRE X-ray 3.17 A/B 1-98 [» ]
3JRF X-ray 3.05 A/B 1-98 [» ]
3JRG X-ray 3.11 A/B 1-98 [» ]
3JRH X-ray 2.88 A/B 1-98 [» ]
3JRI X-ray 3.11 A/B 1-98 [» ]
4FIS X-ray 2.30 A/B 1-98 [» ]
DisProti DP00422.
ProteinModelPortali P0A6R3.
SMRi P0A6R3. Positions 1-98.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47975N.
IntActi P0A6R3. 25 interactions.
MINTi MINT-1225073.
STRINGi 511145.b3261.

Proteomic databases

PaxDbi P0A6R3.
PRIDEi P0A6R3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76293 ; AAC76293 ; b3261 .
BAE77302 ; BAE77302 ; BAE77302 .
GeneIDi 12932870.
947697.
KEGGi ecj:Y75_p3179.
eco:b3261.
PATRICi 32121952. VBIEscCol129921_3360.

Organism-specific databases

EchoBASEi EB0313.
EcoGenei EG10317. fis.

Phylogenomic databases

eggNOGi COG2901.
HOGENOMi HOG000256331.
InParanoidi P0A6R3.
KOi K03557.
OMAi HNQTRAA.
OrthoDBi EOG67HJXZ.
PhylomeDBi P0A6R3.

Enzyme and pathway databases

BioCyci EcoCyc:PD00196.
ECOL316407:JW3229-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6R3.
PROi P0A6R3.

Gene expression databases

Genevestigatori P0A6R3.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
HAMAPi MF_00166. DNA_binding_Fis.
InterProi IPR005412. Fis_DNA-bd.
IPR009057. Homeodomain-like.
IPR002197. HTH_Fis.
[Graphical view ]
Pfami PF02954. HTH_8. 1 hit.
[Graphical view ]
PIRSFi PIRSF002097. DNA-binding_Fis. 1 hit.
PRINTSi PR01591. DNABINDNGFIS.
PR01590. HTHFIS.
SUPFAMi SSF46689. SSF46689. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of the gene encoding the Hin recombinational enhancer binding protein."
    Johnson R.C., Ball C.A., Pfeffer D., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 85:3484-3488(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE.
  2. "Escherichia coli host factor for site-specific DNA inversion: cloning and characterization of the fis gene."
    Koch C., Vanderkerckhove J., Kahmann R.
    Proc. Natl. Acad. Sci. U.S.A. 85:4237-4241(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29.
  3. "Dramatic changes in Fis levels upon nutrient upshift in Escherichia coli."
    Ball C.A., Osuna R., Ferguson K.C., Johnson R.C.
    J. Bacteriol. 174:8043-8056(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The ndh-binding protein (Nbp) regulates the ndh gene of Escherichia coli in response to growth phase and is identical to Fis."
    Green J., Anjum M.F., Guest J.R.
    Mol. Microbiol. 20:1043-1055(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
  7. "E.coli Fis protein activates ribosomal RNA transcription in vitro and in vivo."
    Ross W., Thompson J.F., Newlands J.T., Gourse R.L.
    EMBO J. 9:3733-3742(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The Escherichia coli Fis protein prevents initiation of DNA replication from oriC in vitro."
    Wold S., Crooke E., Skarstad K.
    Nucleic Acids Res. 24:3527-3532(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Identification of two functional regions in Fis: the N-terminus is required to promote Hin-mediated DNA inversion but not lambda excision."
    Osuna R., Finkel S.E., Johnson R.C.
    EMBO J. 10:1593-1603(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, DOMAINS.
  10. "The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome."
    Marianovsky I., Aizenman E., Engelberg-Kulka H., Glaser G.
    J. Biol. Chem. 276:5975-5984(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO THE MAZE-MAZF PROMOTER.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  11. "Three-dimensional structure of the E. coli DNA-binding protein FIS."
    Kostrewa D., Granzin J., Koch C., Choe H.-W., Raghunathan S., Wolf W., Labahn J., Kahmann R., Saenger W.
    Nature 349:178-180(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  12. "Crystal structure of the factor for inversion stimulation FIS at 2.0-A resolution."
    Kostrewa D., Granzin J., Stock D., Choe H.-W., Labahn J., Saenger W.
    J. Mol. Biol. 226:209-226(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  13. "The transactivation region of the fis protein that controls site-specific DNA inversion contains extended mobile beta-hairpin arms."
    Safo M.K., Yang W.Z., Corselli L., Cramton S.E., Yuan H.S., Johnson R.C.
    EMBO J. 16:6860-6873(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
  14. "Structural analysis of the transcriptional activation region on fis: crystal structures of six fis mutants with different activation properties."
    Cheng Y.-S., Yang W.-Z., Johnson R.C., Yuan H.S.
    J. Mol. Biol. 302:1139-1151(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS.

Entry informationi

Entry nameiFIS_ECOLI
AccessioniPrimary (citable) accession number: P0A6R3
Secondary accession number(s): P11028, P37404, Q2M8V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: October 29, 2014
This is version 92 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, Direct protein sequencing, 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

External Data

Dasty 3