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 24-JAN-2024, entry version 151. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 296. DR BioGRID; 852010; 1. DR DIP; DIP-47975N; -. DR IntAct; P0A6R3; 25. DR STRING; 511145.b3261; -. DR jPOST; P0A6R3; -. DR PaxDb; 511145-b3261; -. DR EnsemblBacteria; AAC76293; AAC76293; b3261. 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 OrthoDB; 9802388at2; -. 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:0051276; P:chromosome organization; IDA:EcoCyc. DR GO; GO:0006351; P:DNA-templated transcription; IMP:CAFA. 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 DNA-templated transcription; IDA:EcoCyc. DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc. DR DisProt; DP00422; -. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. 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 PANTHER; PTHR47918; DNA-BINDING PROTEIN FIS; 1. DR PANTHER; PTHR47918:SF1; DNA-BINDING PROTEIN FIS; 1. DR Pfam; PF02954; HTH_8; 1. DR PIRSF; PIRSF002097; DNA-binding_Fis; 1. DR PRINTS; PR01591; DNABINDNGFIS. DR PRINTS; PR01590; HTHFIS. DR SUPFAM; SSF46689; Homeodomain-like; 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 //