| General information | | DisProt: | DP00422 | | Name: | DNA-binding protein fis | | Synonym(s): | FIS_ECOLI
Factor-for-inversion stimulation protein
Hin recombinational enhancer-binding protein
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P0A6R3 | | UniGene: | | | SwissProt: | FIS_ECOLI | | TrEMBL: | | | NCBI (GI): | 68566319 | | Source organism: | Escherichia coli | | Sequence length: | 98 | | Percent disordered: | 26% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MFEQRVNSDV LTVSTVNSQD QVTQKPLRDS VKQALKNYFA QLNGQDVNDL YELVLAEVEQ - 60
PLLDMVMQYT RGNQTRAALM MGINRGTLRK KLKKYGMN
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| Functional narrative |
The factor for inversion stimulation (FIS) is a dimeric DNA-binding protein found in enteric bacteria where it is involved in a number of expression regulation functions, including site-specific DNA inversion as well as the regulation of its own transcription. FIS consists of 98 residues and self-assembles into an entwined dimer containing a flexible and mostly disordered N-terminus followed by four alfa-helices. The positively charged C-terminus is involved in DNA binding, and the N-terminal helix binds Hin and Gin recombinases to stimulate DNA inversion. The disordered N-terminal region of Fis appears to be specific for controlling DNA inversion and probably contacts the DNA invertases to regulate their catalytic activity. Activates ribosomal RNA transcription. 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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | N-terminal region | | Location: | 1 - 25 | | Length: | 25 | | Region sequence: |
MFEQRVNSDVLTVSTVNSQDQVTQK | | Modification type: | Native
| | PDB: | 1ETY:A, 1FIA:A, 3FIS:A | | Structural/functional type: | Function arises from the disordered state
Function arises via an order to disorder transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Transactivation (transcriptional activation)
Protein-protein binding
| Detection methods:
- X-ray crystallography (2.3 Å and 2.0 Å resolution)
| References:
- Cheng YS, Yang WZ, Johnson RC, Yuan HS. "Structural analysis of the transcriptional activation on Fis: crystal structures of six Fis mutants with different activation properties." J Mol Biol. 2000; 302(5): 1139-51. PubMed: 11183780
- Kostrewa D, Granzin J, Stock D, Choe HW, Labahn J, Saenger W. "Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution." J Mol Biol. 1992; 226(1): 209-26. PubMed: 1619650
- Safo MK, Yang WZ, Corselli L, Cramton SE, Yuan HS, Johnson RC. "The transactivation region of the fis protein that controls site-specific DNA inversion contains extended mobile beta-hairpin arms." Embo J. 1997; 16(22): 6860-73. PubMed: 9362499
- Yuan HS, Finkel SE, Feng JA, Kaczor-Grzeskowiak M, Johnson RC, Dickerson RE. "The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding." Proc Natl Acad Sci U S A. 1991; 88(21): 9558-62. PubMed: 1946369
| Comments:A mutant Fis crystal structure reveals that the transactivation domain of Fis contains two beta-hairpin arms that protrude over 20 Å from the protein core (EMBO J. 1997, 16, 6860-6873). The most critical activating residues are located near the tips of the beta-arms.
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| References |
- Travers A, Schneider R, Muskhelishvili G. "DNA supercoiling and transcription in Escherichia coli: The FIS connection." Biochimie. 2001; 83(2): 213-7. PubMed: 11278071
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