FIS_ECOLI
ID FIS_ECOLI Reviewed; 98 AA.
AC P0A6R3; P11028; P37404; Q2M8V4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=DNA-binding protein Fis {ECO:0000255|HAMAP-Rule:MF_00166};
DE AltName: Full=Factor-for-inversion stimulation protein;
DE AltName: Full=Hin recombinational enhancer-binding protein;
GN Name=fis {ECO:0000255|HAMAP-Rule:MF_00166};
GN OrderedLocusNames=b3261, JW3229;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE.
RX PubMed=2835774; DOI=10.1073/pnas.85.10.3484;
RA Johnson R.C., Ball C.A., Pfeffer D., Simon M.I.;
RT "Isolation of the gene encoding the Hin recombinational enhancer binding
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3484-3488(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-29.
RX PubMed=2837762; DOI=10.1073/pnas.85.12.4237;
RA Koch C., Vanderkerckhove J., Kahmann R.;
RT "Escherichia coli host factor for site-specific DNA inversion: cloning and
RT characterization of the fis gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4237-4241(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1459953; DOI=10.1128/jb.174.24.8043-8056.1992;
RA Ball C.A., Osuna R., Ferguson K.C., Johnson R.C.;
RT "Dramatic changes in Fis levels upon nutrient upshift in Escherichia
RT coli.";
RL J. Bacteriol. 174:8043-8056(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-11.
RX PubMed=8809757; DOI=10.1111/j.1365-2958.1996.tb02545.x;
RA Green J., Anjum M.F., Guest J.R.;
RT "The ndh-binding protein (Nbp) regulates the ndh gene of Escherichia coli
RT in response to growth phase and is identical to Fis.";
RL Mol. Microbiol. 20:1043-1055(1996).
RN [7]
RP FUNCTION.
RX PubMed=2209559; DOI=10.1002/j.1460-2075.1990.tb07586.x;
RA Ross W., Thompson J.F., Newlands J.T., Gourse R.L.;
RT "E.coli Fis protein activates ribosomal RNA transcription in vitro and in
RT vivo.";
RL EMBO J. 9:3733-3742(1990).
RN [8]
RP FUNCTION.
RX PubMed=8836178; DOI=10.1093/nar/24.18.3527;
RA Wold S., Crooke E., Skarstad K.;
RT "The Escherichia coli Fis protein prevents initiation of DNA replication
RT from oriC in vitro.";
RL Nucleic Acids Res. 24:3527-3532(1996).
RN [9]
RP MUTAGENESIS, AND DOMAINS.
RX PubMed=1851089; DOI=10.1002/j.1460-2075.1991.tb07680.x;
RA Osuna R., Finkel S.E., Johnson R.C.;
RT "Identification of two functional regions in Fis: the N-terminus is
RT required to promote Hin-mediated DNA inversion but not lambda excision.";
RL EMBO J. 10:1593-1603(1991).
RN [10]
RP BINDING TO THE MAZE-MAZF PROMOTER.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11071896; DOI=10.1074/jbc.m008832200;
RA Marianovsky I., Aizenman E., Engelberg-Kulka H., Glaser G.;
RT "The regulation of the Escherichia coli mazEF promoter involves an unusual
RT alternating palindrome.";
RL J. Biol. Chem. 276:5975-5984(2001).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16963779; DOI=10.1093/nar/gkl542;
RA Grainger D.C., Hurd D., Goldberg M.D., Busby S.J.;
RT "Association of nucleoid proteins with coding and non-coding segments of
RT the Escherichia coli genome.";
RL Nucleic Acids Res. 34:4642-4652(2006).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / BW25993;
RX PubMed=21903814; DOI=10.1126/science.1204697;
RA Wang W., Li G.W., Chen C., Xie X.S., Zhuang X.;
RT "Chromosome organization by a nucleoid-associated protein in live
RT bacteria.";
RL Science 333:1445-1449(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1986310; DOI=10.1038/349178a0;
RA Kostrewa D., Granzin J., Koch C., Choe H.-W., Raghunathan S., Wolf W.,
RA Labahn J., Kahmann R., Saenger W.;
RT "Three-dimensional structure of the E. coli DNA-binding protein FIS.";
RL Nature 349:178-180(1991).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1619650; DOI=10.1016/0022-2836(92)90134-6;
RA Kostrewa D., Granzin J., Stock D., Choe H.-W., Labahn J., Saenger W.;
RT "Crystal structure of the factor for inversion stimulation FIS at 2.0-A
RT resolution.";
RL J. Mol. Biol. 226:209-226(1992).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RX PubMed=9362499; DOI=10.1093/emboj/16.22.6860;
RA Safo M.K., Yang W.Z., Corselli L., Cramton S.E., Yuan H.S., Johnson R.C.;
RT "The transactivation region of the fis protein that controls site-specific
RT DNA inversion contains extended mobile beta-hairpin arms.";
RL EMBO J. 16:6860-6873(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS.
RX PubMed=11183780; DOI=10.1006/jmbi.2000.4123;
RA Cheng Y.-S., Yang W.-Z., Johnson R.C., Yuan H.S.;
RT "Structural analysis of the transcriptional activation region on fis:
RT crystal structures of six fis mutants with different activation
RT properties.";
RL J. Mol. Biol. 302:1139-1151(2000).
CC -!- FUNCTION: Activates ribosomal RNA transcription, as well other genes.
CC Plays a direct role in upstream activation of rRNA promoters. Binds to
CC a recombinational enhancer sequence that is required to stimulate hin-
CC mediated DNA inversion. Prevents initiation of DNA replication from
CC oriC. Binds to hundreds of transcriptionally active and inactive AT-
CC rich sites, approximately half its binding sites are in non-coding DNA,
CC which only accounts for about 10% of the genome (PubMed:16963779).
CC {ECO:0000269|PubMed:16963779, ECO:0000269|PubMed:2209559,
CC ECO:0000269|PubMed:8836178}.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P0A6R3; P30139: thiG; NbExp=3; IntAct=EBI-550170, EBI-547059;
CC P0A6R3; P64503: yebV; NbExp=3; IntAct=EBI-550170, EBI-9126792;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid
CC (PubMed:21903814). {ECO:0000269|PubMed:21903814}.
CC -!- SIMILARITY: Belongs to the transcriptional regulatory Fis family.
CC {ECO:0000255|HAMAP-Rule:MF_00166}.
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DR EMBL; J03245; AAA83856.1; -; Genomic_DNA.
DR EMBL; J03816; AAA98812.1; -; Genomic_DNA.
DR EMBL; M95784; AAA23783.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58065.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76293.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77302.1; -; Genomic_DNA.
DR PIR; A32142; DNECFS.
DR RefSeq; NP_417727.1; NC_000913.3.
DR RefSeq; WP_000462905.1; NZ_STEB01000012.1.
DR PDB; 1ETK; X-ray; 2.10 A; A/B=1-98.
DR PDB; 1ETO; X-ray; 1.90 A; A/B=1-98.
DR PDB; 1ETQ; X-ray; 2.80 A; A/B/C/D=1-98.
DR PDB; 1ETV; X-ray; 2.00 A; A/B=1-98.
DR PDB; 1ETW; X-ray; 2.00 A; A/B=1-98.
DR PDB; 1ETX; X-ray; 1.90 A; A/B=1-98.
DR PDB; 1ETY; X-ray; 2.00 A; A/B=1-98.
DR PDB; 1F36; X-ray; 2.65 A; A/B=1-98.
DR PDB; 1FIA; X-ray; 2.00 A; A/B=1-98.
DR PDB; 1FIP; X-ray; 1.90 A; A/B=1-98.
DR PDB; 3FIS; X-ray; 2.30 A; A/B=1-98.
DR PDB; 3IV5; X-ray; 2.90 A; A/B=1-98.
DR PDB; 3JR9; X-ray; 2.90 A; A/B=1-98.
DR PDB; 3JRA; X-ray; 3.11 A; A/B=1-98.
DR PDB; 3JRB; X-ray; 3.10 A; A/B=1-98.
DR PDB; 3JRC; X-ray; 3.08 A; A/B=1-98.
DR PDB; 3JRD; X-ray; 3.10 A; A/B=1-98.
DR PDB; 3JRE; X-ray; 3.17 A; A/B=1-98.
DR PDB; 3JRF; X-ray; 3.05 A; A/B=1-98.
DR PDB; 3JRG; X-ray; 3.11 A; A/B=1-98.
DR PDB; 3JRH; X-ray; 2.88 A; A/B=1-98.
DR PDB; 3JRI; X-ray; 3.11 A; A/B=1-98.
DR PDB; 4FIS; X-ray; 2.30 A; A/B=1-98.
DR PDB; 5DS9; X-ray; 2.56 A; A/B=1-98.
DR PDB; 5DTD; X-ray; 2.64 A; A/B=1-98.
DR PDB; 5E3L; X-ray; 2.66 A; A/B=1-98.
DR PDB; 5E3M; X-ray; 2.89 A; A/B=1-98.
DR PDB; 5E3N; X-ray; 2.66 A; A/B=1-98.
DR PDB; 5E3O; X-ray; 2.78 A; A/B=1-98.
DR PDB; 6P0S; X-ray; 2.70 A; A/B=1-98.
DR PDB; 6P0T; X-ray; 3.60 A; A/B=1-98.
DR PDB; 6P0U; X-ray; 3.30 A; A/B=1-98.
DR PDBsum; 1ETK; -.
DR PDBsum; 1ETO; -.
DR PDBsum; 1ETQ; -.
DR PDBsum; 1ETV; -.
DR PDBsum; 1ETW; -.
DR PDBsum; 1ETX; -.
DR PDBsum; 1ETY; -.
DR PDBsum; 1F36; -.
DR PDBsum; 1FIA; -.
DR PDBsum; 1FIP; -.
DR PDBsum; 3FIS; -.
DR PDBsum; 3IV5; -.
DR PDBsum; 3JR9; -.
DR PDBsum; 3JRA; -.
DR PDBsum; 3JRB; -.
DR PDBsum; 3JRC; -.
DR PDBsum; 3JRD; -.
DR PDBsum; 3JRE; -.
DR PDBsum; 3JRF; -.
DR PDBsum; 3JRG; -.
DR PDBsum; 3JRH; -.
DR PDBsum; 3JRI; -.
DR PDBsum; 4FIS; -.
DR PDBsum; 5DS9; -.
DR PDBsum; 5DTD; -.
DR PDBsum; 5E3L; -.
DR PDBsum; 5E3M; -.
DR PDBsum; 5E3N; -.
DR PDBsum; 5E3O; -.
DR PDBsum; 6P0S; -.
DR PDBsum; 6P0T; -.
DR PDBsum; 6P0U; -.
DR AlphaFoldDB; P0A6R3; -.
DR SMR; P0A6R3; -.
DR BioGRID; 4261864; 136.
DR BioGRID; 852010; 1.
DR DIP; DIP-47975N; -.
DR IntAct; P0A6R3; 25.
DR STRING; 511145.b3261; -.
DR jPOST; P0A6R3; -.
DR PaxDb; P0A6R3; -.
DR PRIDE; P0A6R3; -.
DR EnsemblBacteria; AAC76293; AAC76293; b3261.
DR EnsemblBacteria; BAE77302; BAE77302; BAE77302.
DR GeneID; 8911232; -.
DR GeneID; 947697; -.
DR KEGG; ecj:JW3229; -.
DR KEGG; eco:b3261; -.
DR PATRIC; fig|1411691.4.peg.3467; -.
DR EchoBASE; EB0313; -.
DR eggNOG; COG2901; Bacteria.
DR HOGENOM; CLU_158040_3_0_6; -.
DR InParanoid; P0A6R3; -.
DR OMA; MVLCEVE; -.
DR PhylomeDB; P0A6R3; -.
DR BioCyc; EcoCyc:PD00196; -.
DR EvolutionaryTrace; P0A6R3; -.
DR PRO; PR:P0A6R3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000770; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0031421; C:invertasome; IMP:CAFA.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0000786; C:nucleosome; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CAFA.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoliWiki.
DR GO; GO:0044374; F:sequence-specific DNA binding, bending; IMP:CAFA.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0045911; P:positive regulation of DNA recombination; IMP:CAFA.
DR GO; GO:0032359; P:provirus excision; IMP:CAFA.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:CAFA.
DR DisProt; DP00422; -.
DR HAMAP; MF_00166; DNA_binding_Fis; 1.
DR InterPro; IPR005412; Fis_DNA-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR Pfam; PF02954; HTH_8; 1.
DR PIRSF; PIRSF002097; DNA-binding_Fis; 1.
DR PRINTS; PR01591; DNABINDNGFIS.
DR PRINTS; PR01590; HTHFIS.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..98
FT /note="DNA-binding protein Fis"
FT /id="PRO_0000203878"
FT DNA_BIND 74..93
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00166"
FT REGION 17..44
FT /note="Required for the stimulation of HIN-mediated
FT recombination"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1ETO"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3JRD"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1ETO"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:1ETO"
FT HELIX 50..69
FT /evidence="ECO:0007829|PDB:1ETO"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1ETO"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:1ETO"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1ETO"
SQ SEQUENCE 98 AA; 11240 MW; 2E339BFCFCDB163C CRC64;
MFEQRVNSDV LTVSTVNSQD QVTQKPLRDS VKQALKNYFA QLNGQDVNDL YELVLAEVEQ
PLLDMVMQYT RGNQTRAALM MGINRGTLRK KLKKYGMN
