HNS_ECOLI
ID HNS_ECOLI Reviewed; 137 AA.
AC P0ACF8; P08936; Q47267;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA-binding protein H-NS {ECO:0000303|PubMed:2841565};
DE AltName: Full=Heat-stable nucleoid-structuring protein {ECO:0000303|PubMed:6395665};
DE AltName: Full=Histone-like protein HLP-II;
DE AltName: Full=Protein B1 {ECO:0000303|PubMed:333393};
DE AltName: Full=Protein H1 {ECO:0000303|PubMed:4566454};
GN Name=hns {ECO:0000303|PubMed:2841565};
GN Synonyms=bglY {ECO:0000303|PubMed:2177526}, cur,
GN drdX {ECO:0000303|PubMed:1691451}, hnsA, msyA {ECO:0000303|PubMed:1537791},
GN osmZ {ECO:0000303|PubMed:2177526}, pilG, topS;
GN OrderedLocusNames=b1237, JW1225;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2841565; DOI=10.1007/bf00334684;
RA Pon C.L., Calogero R.A., Gualerzi C.O.;
RT "Identification, cloning, nucleotide sequence and chromosomal map location
RT of hns, the structural gene for Escherichia coli DNA-binding protein H-
RT NS.";
RL Mol. Gen. Genet. 212:199-202(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RX PubMed=3135462; DOI=10.1111/j.1365-2958.1988.tb00035.x;
RA Falconi M., Gualtieri M.T., la Teana A., Losso M.A., Pon C.L.;
RT "Proteins from the prokaryotic nucleoid: primary and quaternary structure
RT of the 15-kD Escherichia coli DNA binding protein H-NS.";
RL Mol. Microbiol. 2:323-329(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=1691451; DOI=10.1038/344682a0;
RA Goeransson M., Sonden B., Nilsson P., Dagberg B., Forsman K.,
RA Emanuelsson K., Uhlin B.E.;
RT "Transcriptional silencing and thermoregulation of gene expression in
RT Escherichia coli.";
RL Nature 344:682-685(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1537791; DOI=10.1128/jb.174.5.1454-1461.1992;
RA Ueguchi C., Ito K.;
RT "Multicopy suppression: an approach to understanding intracellular
RT functioning of the protein export system.";
RL J. Bacteriol. 174:1454-1461(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100;
RX PubMed=2177526; DOI=10.1007/bf00259454;
RA May G., Dersch P., Haardt M., Middendorf A., Bremer E.;
RT "The osmZ (bglY) gene encodes the DNA-binding protein H-NS (H1a), a
RT component of the Escherichia coli K12 nucleoid.";
RL Mol. Gen. Genet. 224:81-90(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=K12;
RX PubMed=7773397; DOI=10.1099/13500872-141-4-959;
RA Danchin A., Krin E.;
RT "Filling the gap between hns and adhE in Escherichia coli K12.";
RL Microbiology 141:959-960(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=2494066; DOI=10.1016/0014-5793(89)81156-1;
RA la Teana A., Falconi M., Scarlato V., Lammi M., Pon C.L.;
RT "Characterization of the structural genes for the DNA-binding protein H-NS
RT in Enterobacteriaceae.";
RL FEBS Lett. 244:34-38(1989).
RN [11]
RP PROTEIN SEQUENCE OF 2-27, AND SUBUNIT.
RC STRAIN=P4X8 / ME7784;
RX PubMed=2020545; DOI=10.1093/nar/19.5.1063;
RA Kajitani M., Ishihama A.;
RT "Identification and sequence determination of the host factor gene for
RT bacteriophage Q beta.";
RL Nucleic Acids Res. 19:1063-1066(1991).
RN [12]
RP PROTEIN SEQUENCE OF 2-21, AND DNA-BINDING.
RC STRAIN=MRE-600;
RX PubMed=6370250; DOI=10.1016/0006-291x(84)90895-7;
RA Laine B., Sautiere P., Spassky A., Rimsky S.;
RT "A DNA-binding protein from E. coli isolation, characterization and its
RT relationship with proteins H1 and B1.";
RL Biochem. Biophys. Res. Commun. 119:1147-1153(1984).
RN [13]
RP PROTEIN SEQUENCE OF 2-20, AND DNA-BINDING.
RX PubMed=2126011; DOI=10.1093/oxfordjournals.jbchem.a123216;
RA Yamada H., Muramatsu S., Mizuno T.;
RT "An Escherichia coli protein that preferentially binds to sharply curved
RT DNA.";
RL J. Biochem. 108:420-425(1990).
RN [14]
RP PROTEIN SEQUENCE OF 2-20.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [15]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [16]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [17]
RP PROTEIN SEQUENCE OF 2-8, DNA-BINDING, AND PROTEIN NAME.
RX PubMed=6395665; DOI=10.1007/978-1-4684-8730-5_48;
RA Lammi M., Paci M., Pon C.L., Losso M.A., Miano A., Pawlik R.T.,
RA Gianfranceschi G.L., Gualerzi C.O.;
RT "Proteins from the prokaryotic nucleoid: biochemical and 1H NMR studies on
RT three bacterial histone-like proteins.";
RL Adv. Exp. Med. Biol. 179:467-477(1984).
RN [18]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [19]
RP FUNCTION, SUBUNIT, AND DNA-BINDING.
RC STRAIN=MRE-600;
RX PubMed=4566454; DOI=10.1073/pnas.69.12.3643;
RA Cukier-Kahn R., Jacquet M., Gros F.;
RT "Two heat-resistant, low molecular weight proteins from Escherichia coli
RT that stimulate DNA-directed RNA synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 69:3643-3647(1972).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RC STRAIN=802;
RX PubMed=333393; DOI=10.1093/nar/4.8.2725;
RA Varshavsky A.J., Nedospasov S.A., Bakayev V.V., Bakayeva T.G.,
RA Georgiev G.P.;
RT "Histone-like proteins in the purified Escherichia coli
RT deoxyribonucleoprotein.";
RL Nucleic Acids Res. 4:2725-2745(1977).
RN [21]
RP SUBUNIT, AND DNA-BINDING.
RC STRAIN=MRE-600;
RX PubMed=338303; DOI=10.1111/j.1432-1033.1977.tb11929.x;
RA Spassky A., Buc H.C.;
RT "Physico-chemical properties of a DNA binding protein: Escherichia coli
RT factor H1.";
RL Eur. J. Biochem. 81:79-90(1977).
RN [22]
RP FUNCTION, INDUCTION, POST-TRANSLATIONAL MODIFICATION, AND DNA-BINDING.
RC STRAIN=MRE-600;
RX PubMed=6379600; DOI=10.1093/nar/12.13.5321;
RA Spassky A., Rimsky S., Garreau H., Buc H.;
RT "H1a, an E. coli DNA-binding protein which accumulates in stationary phase,
RT strongly compacts DNA in vitro.";
RL Nucleic Acids Res. 12:5321-5340(1984).
RN [23]
RP FUNCTION, AND BINDING OF CURVED DNA.
RX PubMed=2512122; DOI=10.1002/j.1460-2075.1989.tb08615.x;
RA Bracco L., Kotlarz D., Kolb A., Diekmann S., Buc H.;
RT "Synthetic curved DNA sequences can act as transcriptional activators in
RT Escherichia coli.";
RL EMBO J. 8:4289-4296(1989).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2128918; DOI=10.1016/0300-9084(90)90008-5;
RA Bertin P., Lejeune P., Laurent-Winter C., Danchin A.;
RT "Mutations in bglY, the structural gene for the DNA-binding protein H1,
RT affect expression of several Escherichia coli genes.";
RL Biochimie 72:889-891(1990).
RN [25]
RP FUNCTION, INDUCTION, AND DNA-BINDING.
RX PubMed=7934818; DOI=10.1111/j.1365-2958.1993.tb01953.x;
RA Falconi M., Higgins P.N., Spurio R., Pon C.L., Gualerzi C.O.;
RT "Expression of the gene encoding the major bacterial nucleotide protein H-
RT NS is subject to transcriptional auto-repression.";
RL Mol. Microbiol. 10:273-282(1993).
RN [26]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8226663; DOI=10.1128/jb.175.22.7170-7177.1993;
RA Welch T.J., Farewell A., Neidhardt F.C., Bartlett D.H.;
RT "Stress response of Escherichia coli to elevated hydrostatic pressure.";
RL J. Bacteriol. 175:7170-7177(1993).
RN [27]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-26; 53-GLU--THR-55;
RP 64-MET--GLN-137; TYR-97; THR-110; GLY-113; PRO-116; ILE-119;
RP 122-ALA--GLN-137 AND PHE-133.
RX PubMed=8755860; DOI=10.1128/jb.178.15.4335-4343.1996;
RA Williams R.M., Rimsky S., Buc H.;
RT "Probing the structure, function, and interactions of the Escherichia coli
RT H-NS and StpA proteins by using dominant negative derivatives.";
RL J. Bacteriol. 178:4335-4343(1996).
RN [28]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12, K12 / MC1029, and K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8890170; DOI=10.1002/j.1460-2075.1996.tb00877.x;
RA Sonden B., Uhlin B.E.;
RT "Coordinated and differential expression of histone-like proteins in
RT Escherichia coli: regulation and function of the H-NS analog StpA.";
RL EMBO J. 15:4970-4980(1996).
RN [29]
RP INDUCTION BY COLD-SHOCK.
RC STRAIN=CSH142;
RX PubMed=8898389; DOI=10.1111/j.1365-2958.1996.tb02582.x;
RA Jones P.G., Inouye M.;
RT "RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose
RT absence triggers the cold-shock response.";
RL Mol. Microbiol. 21:1207-1218(1996).
RN [30]
RP FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-12;
RP ARG-15; ARG-54; ARG-90; ALA-91; 92-GLN--GLN-137; ARG-93; PRO-94; ALA-95;
RP THR-110; GLY-111; ARG-114 AND THR-115.
RC STRAIN=K12 / CSH26;
RX PubMed=8913298; DOI=10.1006/jmbi.1996.0566;
RA Ueguchi C., Suzuki T., Yoshida T., Tanaka K., Mizuno T.;
RT "Systematic mutational analysis revealing the functional domain
RT organization of Escherichia coli nucleoid protein H-NS.";
RL J. Mol. Biol. 263:149-162(1996).
RN [31]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [32]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 2-SER--GLY-69; 2-SER--GLU-20;
RP LEU-30; 64-MET--GLN-137 AND 92-GLN--GLN-137.
RX PubMed=9398522; DOI=10.1006/jmbi.1997.1381;
RA Ueguchi C., Seto C., Suzuki T., Mizuno T.;
RT "Clarification of the dimerization domain and its functional significance
RT for the Escherichia coli nucleoid protein H-NS.";
RL J. Mol. Biol. 274:145-151(1997).
RN [33]
RP FUNCTION IN DNA COMPACTION, AND DNA-BINDING.
RX PubMed=10982869; DOI=10.1093/nar/28.18.3504;
RA Dame R.T., Wyman C., Goosen N.;
RT "H-NS mediated compaction of DNA visualised by atomic force microscopy.";
RL Nucleic Acids Res. 28:3504-3510(2000).
RN [34]
RP FUNCTION IN FLAGELLA BIOGENESIS AND MOTILITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11031114; DOI=10.1006/jmbi.2000.4147;
RA Ko M., Park C.;
RT "Two novel flagellar components and H-NS are involved in the motor function
RT of Escherichia coli.";
RL J. Mol. Biol. 303:371-382(2000).
RN [35]
RP POSSIBLE MECHANISM OF TRANSCRIPTIONAL REPRESSION.
RX PubMed=11714691; DOI=10.1074/jbc.c100603200;
RA Dame R.T., Wyman C., Wurm R., Wagner R., Goosen N.;
RT "Structural basis for H-NS-mediated trapping of RNA polymerase in the open
RT initiation complex at the rrnB P1.";
RL J. Biol. Chem. 277:2146-2150(2002).
RN [36]
RP INTERACTION WITH HHA, MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=11790731; DOI=10.1128/jb.184.3.629-635.2002;
RA Nieto J.M., Madrid C., Miquelay E., Parra J.L., Rodriguez S., Juarez A.;
RT "Evidence for direct protein-protein interaction between members of the
RT enterobacterial Hha/YmoA and H-NS families of proteins.";
RL J. Bacteriol. 184:629-635(2002).
RN [37]
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-12 AND ARG-15.
RX PubMed=16650431; DOI=10.1016/j.jmb.2006.03.059;
RA Garcia J., Madrid C., Juarez A., Pons M.;
RT "New roles for key residues in helices H1 and H2 of the Escherichia coli H-
RT NS N-terminal domain: H-NS dimer stabilization and Hha binding.";
RL J. Mol. Biol. 359:679-689(2006).
RN [38]
RP FUNCTION, REGULON, 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 [39]
RP FUNCTION IN SILENCING OF FOREIGN DNA, REGULON, AND DNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17046956; DOI=10.1093/dnares/dsl009;
RA Oshima T., Ishikawa S., Kurokawa K., Aiba H., Ogasawara N.;
RT "Escherichia coli histone-like protein H-NS preferentially binds to
RT horizontally acquired DNA in association with RNA polymerase.";
RL DNA Res. 13:141-153(2006).
RN [40]
RP ROLE IN CURLI FIMBRIAE EXPRESSION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=17010156; DOI=10.1111/j.1365-2958.2006.05440.x;
RA Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.;
RT "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia
RT coli.";
RL Mol. Microbiol. 62:1014-1034(2006).
RN [41]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=17435766; DOI=10.1038/nsmb1233;
RA Bouffartigues E., Buckle M., Badaut C., Travers A., Rimsky S.;
RT "H-NS cooperative binding to high-affinity sites in a regulatory element
RT results in transcriptional silencing.";
RL Nat. Struct. Mol. Biol. 14:441-448(2007).
RN [42]
RP FUNCTION, MODEL OF ACTION, AND DNA-BINDING.
RX PubMed=17881364; DOI=10.1093/nar/gkm712;
RA Lang B., Blot N., Bouffartigues E., Buckle M., Geertz M., Gualerzi C.O.,
RA Mavathur R., Muskhelishvili G., Pon C.L., Rimsky S., Stella S., Babu M.M.,
RA Travers A.;
RT "High-affinity DNA binding sites for H-NS provide a molecular basis for
RT selective silencing within proteobacterial genomes.";
RL Nucleic Acids Res. 35:6330-6337(2007).
RN [43]
RP FUNCTION IN REPRESSING CRISPR EXPRESSION.
RC STRAIN=K12;
RX PubMed=20132443; DOI=10.1111/j.1365-2958.2010.07073.x;
RA Pul U., Wurm R., Arslan Z., Geissen R., Hofmann N., Wagner R.;
RT "Identification and characterization of E. coli CRISPR-cas promoters and
RT their silencing by H-NS.";
RL Mol. Microbiol. 75:1495-1512(2010).
RN [44]
RP FUNCTION IN TRANSLATION ACTIVATION, AND MRNA-BINDING.
RX PubMed=20595230; DOI=10.1101/gad.576310;
RA Park H.S., Ostberg Y., Johansson J., Wagner E.G., Uhlin B.E.;
RT "Novel role for a bacterial nucleoid protein in translation of mRNAs with
RT suboptimal ribosome-binding sites.";
RL Genes Dev. 24:1345-1350(2010).
RN [45]
RP FUNCTION, ANTAGONIZED BY LEUO, ROLE IN CRISPR EXPRESSION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=20659289; DOI=10.1111/j.1365-2958.2010.07315.x;
RA Westra E.R., Pul U., Heidrich N., Jore M.M., Lundgren M., Stratmann T.,
RA Wurm R., Raine A., Mescher M., Van Heereveld L., Mastop M., Wagner E.G.,
RA Schnetz K., Van Der Oost J., Wagner R., Brouns S.J.;
RT "H-NS-mediated repression of CRISPR-based immunity in Escherichia coli K12
RT can be relieved by the transcription activator LeuO.";
RL Mol. Microbiol. 77:1380-1393(2010).
RN [46]
RP INTERACTION WITH HHA AND CNU (YDGT), AND MUTAGENESIS OF ARG-12.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21600204; DOI=10.1016/j.febslet.2011.05.024;
RA de Alba C.F., Solorzano C., Paytubi S., Madrid C., Juarez A., Garcia J.,
RA Pons M.;
RT "Essential residues in the H-NS binding site of Hha, a co-regulator of
RT horizontally acquired genes in Enterobacteria.";
RL FEBS Lett. 585:1765-1770(2011).
RN [47]
RP FUNCTION IN CHROMOSOME ORGANIZATION, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LEU-30 AND PRO-116.
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 [48]
RP FUNCTION, REGULON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=23543115; DOI=10.1093/dnares/dst008;
RA Ueda T., Takahashi H., Uyar E., Ishikawa S., Ogasawara N., Oshima T.;
RT "Functions of the Hha and YdgT proteins in transcriptional silencing by the
RT nucleoid proteins, H-NS and StpA, in Escherichia coli.";
RL DNA Res. 20:263-271(2013).
RN [49]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24449106; DOI=10.1101/gad.234336.113;
RA Singh S.S., Singh N., Bonocora R.P., Fitzgerald D.M., Wade J.T.,
RA Grainger D.C.;
RT "Widespread suppression of intragenic transcription initiation by H-NS.";
RL Genes Dev. 28:214-219(2014).
RN [50]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=26789284; DOI=10.1371/journal.pgen.1005796;
RA Higashi K., Tobe T., Kanai A., Uyar E., Ishikawa S., Suzuki Y.,
RA Ogasawara N., Kurokawa K., Oshima T.;
RT "H-NS facilitates sequence diversification of horizontally transferred DNAs
RT during their integration in host chromosomes.";
RL PLoS Genet. 12:E1005796-E1005796(2016).
RN [51]
RP HYDROXYBUTYRYLATION AT LYS-121, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP LYS-96 AND LYS-121.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=34903851; DOI=10.1038/s41589-021-00906-3;
RA Dong H., Zhao Y., Bi C., Han Y., Zhang J., Bai X., Zhai G., Zhang H.,
RA Tian S., Hu D., Xu L., Zhang K.;
RT "TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate
RT transcription.";
RL Nat. Chem. Biol. 18:142-151(2022).
RN [52]
RP STRUCTURE BY NMR OF 91-137.
RX PubMed=7875316; DOI=10.1016/0014-5793(95)00079-o;
RA Shindo H., Iwaki T., Ieda R., Kurumizaka H., Ueguchi C., Mizuno T.,
RA Morikawa S., Nakamura H., Kuboniwa H.;
RT "Solution structure of the DNA binding domain of a nucleoid-associated
RT protein, H-NS, from Escherichia coli.";
RL FEBS Lett. 360:125-131(1995).
RN [53]
RP STRUCTURE BY NMR OF 2-58, DOMAIN, MUTAGENESIS OF LYS-6 AND GLN-17, AND
RP COILED COIL.
RX PubMed=12460581; DOI=10.1016/s0022-2836(02)01141-5;
RA Esposito D., Petrovic A., Harris R., Ono S., Eccleston J.F., Mbabaali A.,
RA Haq I., Higgins C.F., Hinton J.C., Driscoll P.C., Ladbury J.E.;
RT "H-NS oligomerization domain structure reveals the mechanism for high order
RT self-association of the intact protein.";
RL J. Mol. Biol. 324:841-850(2002).
RN [54]
RP STRUCTURE BY NMR OF 2-47, DOMAIN, MUTAGENESIS OF 12-ARG--ARG-15, AND COILED
RP COIL.
RX PubMed=12592399; DOI=10.1038/nsb904;
RA Bloch V., Yang Y., Margeat E., Chavanieu A., Auge M.T., Robert B.,
RA Arold S., Rimsky S., Kochoyan M.;
RT "The H-NS dimerization domain defines a new fold contributing to DNA
RT recognition.";
RL Nat. Struct. Biol. 10:212-218(2003).
RN [55]
RP STRUCTURE BY SOLID STATE NMR, SUBUNIT, AND DOMAIN.
RX PubMed=23601147; DOI=10.1111/febs.12297;
RA Renault M., Garcia J., Cordeiro T.N., Baldus M., Pons M.;
RT "Protein oligomers studied by solid-state NMR--the case of the full-length
RT nucleoid-associated protein histone-like nucleoid structuring protein.";
RL FEBS J. 280:2916-2928(2013).
RN [56]
RP STRUCTURE BY NMR OF 1-46 IN COMPLEX WITH HHA, SUBUNIT, AND MUTAGENESIS OF
RP LYS-32.
RX PubMed=26085102; DOI=10.1074/jbc.m114.630400;
RA Cordeiro T.N., Garcia J., Bernado P., Millet O., Pons M.;
RT "A three-protein charge zipper stabilizes a complex modulating bacterial
RT gene silencing.";
RL J. Biol. Chem. 290:21200-21212(2015).
RN [57]
RP REVIEW.
RX PubMed=25638302; DOI=10.1016/j.mib.2015.01.009;
RA Landick R., Wade J.T., Grainger D.C.;
RT "H-NS and RNA polymerase: a love-hate relationship?";
RL Curr. Opin. Microbiol. 24:53-59(2015).
CC -!- FUNCTION: A DNA-binding protein implicated in transcriptional
CC repression (silencing) (PubMed:333393, PubMed:2128918, PubMed:8890170,
CC PubMed:8913298, PubMed:9398522, PubMed:16963779, PubMed:17046956,
CC PubMed:23543115). Also involved in bacterial chromosome organization
CC and compaction (PubMed:6379600, PubMed:10982869, PubMed:21903814). H-NS
CC binds tightly to AT-rich dsDNA and inhibits transcription
CC (PubMed:2512122, PubMed:16963779, PubMed:17435766, PubMed:17881364,
CC PubMed:23543115). Binds upstream and downstream of initiating RNA
CC polymerase, trapping it in a loop and preventing transcription
CC (PubMed:11714691). Binds to hundreds of sites, approximately half its
CC binding sites are in non-coding DNA, which only accounts for about 10%
CC of the genome (PubMed:16963779, PubMed:17046956, PubMed:23543115). Many
CC of these loci were horizontally transferred (HTG); this offers the
CC selective advantage of silencing foreign DNA while keeping it in the
CC genome in case of need (PubMed:17046956, PubMed:17881364,
CC PubMed:26789284). Suppresses transcription at many intragenic sites as
CC well as transcription of spurious, non-coding RNAs genome-wide
CC (PubMed:24449106). Repression of HTG by H-NS is thought to allow their
CC DNA to evolve faster than non-H-NS-bound regions, and facilitates
CC integration of HTG into transcriptional regulatory networks
CC (PubMed:26789284). A subset of H-NS/StpA-regulated genes also require
CC Hha (and/or Cnu, ydgT) for repression; Hha and Cnu increase the number
CC of genes DNA bound by H-NS/StpA and may also modulate the
CC oligomerization of the H-NS/StpA-complex (PubMed:23543115). The protein
CC forms 2 clusters in the nucleoid which gather hns-bound loci together,
CC bridging non-contiguous DNA, and causes DNA substantial condensation
CC (PubMed:21903814). Binds DNA better at low temperatures than at 37
CC degrees Celsius; AT-rich sites nucleate H-NS binding, further DNA-
CC binding is cooperative and this cooperativity decreases with rising
CC temperature (PubMed:17435766, PubMed:17881364). Transcriptional
CC repression can be inhibited by dominant-negative mutants of StpA or
CC itself (PubMed:8755860). May affect transcriptional elongation
CC (PubMed:25638302). Can increase translational efficiency of mRNA with
CC suboptimal Shine-Dalgarno sequences (PubMed:20595230). Plays a role in
CC the thermal control of pili and adhesive curli fimbriae production, by
CC inducing transcription of csgD (PubMed:17010156). Plays a role in
CC flagellar function (PubMed:11031114). Represses the CRISPR-cas
CC promoters, permits only weak transcription of the crRNA precursor; its
CC repression is antagonized by LeuO (PubMed:20132443, PubMed:20659289).
CC Binds preferentially to the upstream region of its own gene recognizing
CC two segments of DNA on both sides of a bend centered around -150
CC (PubMed:7934818). Overexpression suppresses secY24, a temperature-
CC sensitive mutation (PubMed:1537791). Has also been reported to activate
CC transcription of some genes (PubMed:4566454, PubMed:338303,
CC PubMed:2128918). {ECO:0000269|PubMed:10982869,
CC ECO:0000269|PubMed:11031114, ECO:0000269|PubMed:11714691,
CC ECO:0000269|PubMed:1537791, ECO:0000269|PubMed:16963779,
CC ECO:0000269|PubMed:17010156, ECO:0000269|PubMed:17046956,
CC ECO:0000269|PubMed:17435766, ECO:0000269|PubMed:17881364,
CC ECO:0000269|PubMed:20132443, ECO:0000269|PubMed:20595230,
CC ECO:0000269|PubMed:20659289, ECO:0000269|PubMed:2128918,
CC ECO:0000269|PubMed:21903814, ECO:0000269|PubMed:23543115,
CC ECO:0000269|PubMed:24449106, ECO:0000269|PubMed:2512122,
CC ECO:0000269|PubMed:26789284, ECO:0000269|PubMed:333393,
CC ECO:0000269|PubMed:338303, ECO:0000269|PubMed:4566454,
CC ECO:0000269|PubMed:6379600, ECO:0000269|PubMed:7934818,
CC ECO:0000269|PubMed:8755860, ECO:0000269|PubMed:8890170,
CC ECO:0000269|PubMed:8913298, ECO:0000269|PubMed:9398522,
CC ECO:0000305|PubMed:25638302}.
CC -!- ACTIVITY REGULATION: Hydroxyisobutyrylation on Lys-121 (K121hib)
CC decreases the DNA-binding activity of H-NS, promotes the expression of
CC acid-resistance genes and enhances bacterial survival under extreme
CC acid stress. {ECO:0000269|PubMed:34903851}.
CC -!- SUBUNIT: Homodimer, also found as tetramers or higher oligomers
CC (PubMed:4566454, PubMed:338303, PubMed:3135462, PubMed:8913298,
CC PubMed:9398522, PubMed:8755860, PubMed:12460581, PubMed:23601147).
CC Oligomerizes into higher-order complexes that form bridges between
CC adjacent DNA helices. The N-terminal region (residues 1-64) can
CC interact with overexpressed StpA (PubMed:8755860). Forms a complex with
CC Cnu (YdgT) (PubMed:21600204). The H-NS dimer forms a heterotrimeric
CC complex with Hha in the absence of DNA; this is mediated by residues 1-
CC 46 (PubMed:21600204, PubMed:11790731, PubMed:16650431,
CC PubMed:26085102). Interacts with Hfq (PubMed:2020545).
CC {ECO:0000269|PubMed:11790731, ECO:0000269|PubMed:16650431,
CC ECO:0000269|PubMed:2020545, ECO:0000269|PubMed:21600204,
CC ECO:0000269|PubMed:23601147, ECO:0000269|PubMed:26085102,
CC ECO:0000269|PubMed:3135462, ECO:0000269|PubMed:338303,
CC ECO:0000269|PubMed:4566454, ECO:0000269|PubMed:8755860,
CC ECO:0000269|PubMed:8913298, ECO:0000269|PubMed:9398522,
CC ECO:0000305|PubMed:12460581}.
CC -!- INTERACTION:
CC P0ACF8; P64467: cnu; NbExp=3; IntAct=EBI-544934, EBI-551907;
CC P0ACF8; P0ACE3: hha; NbExp=5; IntAct=EBI-544934, EBI-1122578;
CC P0ACF8; P0ACF8: hns; NbExp=10; IntAct=EBI-544934, EBI-544934;
CC P0ACF8; P0ACG1: stpA; NbExp=4; IntAct=EBI-544934, EBI-551928;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814,
CC ECO:0000269|PubMed:333393}. Note=Forms 2 compact clusters per
CC chromosome, located at one-quarter and three-quarter positions on the
CC cell's long axis: 2 H-NS-repressed genes were closely associated with
CC H-NS clusters while a non-H-NS-repressed gene was not substantially
CC associated with the H-NS cluster (PubMed:21903814).
CC {ECO:0000269|PubMed:21903814}.
CC -!- INDUCTION: Protein levels rise from about 4,000/cell in exponential
CC phase to about 18,000/cell in late stationary phase (at protein level)
CC (PubMed:6379600). Subject to transcriptional auto-repression
CC (PubMed:7934818). Induced by increased hydrostatic pressure
CC (PubMed:8226663). hns transcription can be repressed by overexpressed
CC StpA (which is usually repressed by hns) (PubMed:8890170). Induced by
CC cold shock (42 to 15 degrees Celsius) (at protein level)
CC (PubMed:8898389). {ECO:0000269|PubMed:6379600,
CC ECO:0000269|PubMed:7934818, ECO:0000269|PubMed:8226663,
CC ECO:0000269|PubMed:8890170, ECO:0000269|PubMed:8898389}.
CC -!- DOMAIN: A central region (about residues 21-47) is involved in
CC dimerization, but multimerization requires other residues
CC (PubMed:8755860, PubMed:9398522, PubMed:16650431, PubMed:12460581,
CC PubMed:12592399). The dimerization domain (1-47) also acts as a hinge;
CC changes in its structure probably impact oligomerization and DNA-
CC binding geometries (PubMed:23601147). The N-terminus also interacts
CC with Hha, perhaps via residues 2-18; a well-folded dimer is not
CC necessary for Hha binding (PubMed:16650431). The C-terminus (residues
CC 92-137) binds DNA (PubMed:8913298). Residues in the N-terminus
CC contribute to DNA-binding and to discrimination between curved and non-
CC curved DNA (PubMed:12592399). {ECO:0000269|PubMed:12460581,
CC ECO:0000269|PubMed:12592399, ECO:0000269|PubMed:16650431,
CC ECO:0000269|PubMed:23601147, ECO:0000269|PubMed:8755860,
CC ECO:0000269|PubMed:8913298, ECO:0000269|PubMed:9398522}.
CC -!- PTM: 2-hydroxyisobutyrylated by TmcA on Lys-121.
CC {ECO:0000269|PubMed:34903851}.
CC -!- PTM: Cells (strain MRE-600) in mid-exponential phase have three 15.5
CC kDa proteins with 3 different isoelectric points; the major form (H1a,
CC pI 7.5) rises in concentration during growth while the 2 minor forms
CC (H1b, pI about 7.2 and H1c, pI 7.0) remain approximately constant
CC (PubMed:6379600). {ECO:0000269|PubMed:6379600}.
CC -!- MASS SPECTROMETRY: Mass=15407.8; Method=MALDI; Note=A second experiment
CC gave a mass of 15410.1.; Evidence={ECO:0000269|PubMed:11790731};
CC -!- DISRUPTION PHENOTYPE: Decreased growth below 30 degrees Celsius
CC (PubMed:1691451). Altered expression of a number of genes
CC (PubMed:2128918, PubMed:8890170, PubMed:8913298, PubMed:23543115).
CC Derepression of the cryptic blg operon (PubMed:8913298,
CC PubMed:11790731). Alteration of chromosome organization
CC (PubMed:21903814). Double hns-stpA mutants grow slower and have reduced
CC viable cell counts compared to single hns mutants in MC1029 and MC4100
CC backgrounds (PubMed:8890170). In 0.3M NaCl a double hns-stpA deletion
CC up-regulates 583 and down-regulates 86 genes, 363 of which are thought
CC to have been horizontally acquired; 131 are also up-regulated in a
CC double cnu-hha deletion (PubMed:23543115). At 28 degrees Celsius csgD
CC transcription is reduced (PubMed:17010156). Flagella loss due to
CC reduced expression of the flhDC operon (PubMed:11031114). Flagella can
CC be restored by expression of flhDC, but strains are non-motile,
CC suggesting H-NS also plays a role in flagellar function
CC (PubMed:11031114). Disruption leads to increased expression of CRISPR-
CC cas genes and increased viral resistance (PubMed:20659289).
CC {ECO:0000269|PubMed:11031114, ECO:0000269|PubMed:11790731,
CC ECO:0000269|PubMed:1691451, ECO:0000269|PubMed:17010156,
CC ECO:0000269|PubMed:20659289, ECO:0000269|PubMed:2128918,
CC ECO:0000269|PubMed:21903814, ECO:0000269|PubMed:23543115,
CC ECO:0000269|PubMed:8890170, ECO:0000269|PubMed:8913298}.
CC -!- SIMILARITY: Belongs to the histone-like protein H-NS family.
CC {ECO:0000305}.
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DR EMBL; X07688; CAA30530.1; -; Genomic_DNA.
DR EMBL; X59940; CAA42565.1; -; Genomic_DNA.
DR EMBL; X57231; CAA40507.1; -; Genomic_DNA.
DR EMBL; X67326; CAA47740.1; -; Genomic_DNA.
DR EMBL; Y00976; CAA68786.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74319.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36117.1; -; Genomic_DNA.
DR PIR; S00903; S00903.
DR RefSeq; NP_415753.1; NC_000913.3.
DR RefSeq; WP_001287378.1; NZ_STEB01000005.1.
DR PDB; 1HNR; NMR; -; A=91-137.
DR PDB; 1HNS; NMR; -; A=91-137.
DR PDB; 1LR1; NMR; -; A/B=2-58.
DR PDB; 1NI8; NMR; -; A/B=2-47.
DR PDB; 2MW2; NMR; -; B/C=1-47.
DR PDBsum; 1HNR; -.
DR PDBsum; 1HNS; -.
DR PDBsum; 1LR1; -.
DR PDBsum; 1NI8; -.
DR PDBsum; 2MW2; -.
DR AlphaFoldDB; P0ACF8; -.
DR BMRB; P0ACF8; -.
DR SMR; P0ACF8; -.
DR BioGRID; 4263496; 155.
DR BioGRID; 850196; 2.
DR ComplexPortal; CPX-1965; H-NS complex, dimeric.
DR ComplexPortal; CPX-1966; H-NS complex, tetrameric.
DR ComplexPortal; CPX-1979; H-NS-Hha transcription factor complex.
DR ComplexPortal; CPX-1980; H-NS-Cnu transcription factor complex.
DR DIP; DIP-35853N; -.
DR IntAct; P0ACF8; 54.
DR MINT; P0ACF8; -.
DR STRING; 511145.b1237; -.
DR SWISS-2DPAGE; P0ACF8; -.
DR jPOST; P0ACF8; -.
DR PaxDb; P0ACF8; -.
DR PRIDE; P0ACF8; -.
DR EnsemblBacteria; AAC74319; AAC74319; b1237.
DR EnsemblBacteria; BAA36117; BAA36117; BAA36117.
DR GeneID; 66674941; -.
DR GeneID; 945829; -.
DR KEGG; ecj:JW1225; -.
DR KEGG; eco:b1237; -.
DR PATRIC; fig|1411691.4.peg.1048; -.
DR EchoBASE; EB0452; -.
DR eggNOG; COG2916; Bacteria.
DR HOGENOM; CLU_117503_0_0_6; -.
DR OMA; NGVEKTW; -.
DR PhylomeDB; P0ACF8; -.
DR BioCyc; EcoCyc:PD00288; -.
DR EvolutionaryTrace; P0ACF8; -.
DR PHI-base; PHI:6369; -.
DR PRO; PR:P0ACF8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000830; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990121; C:H-NS complex; IPI:ComplexPortal.
DR GO; GO:0036411; C:H-NS-Cnu complex; IPI:ComplexPortal.
DR GO; GO:0097495; C:H-NS-Hha complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0005667; C:transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0003681; F:bent DNA binding; IDA:EcoliWiki.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0036386; P:bacterial nucleoid packaging; IDA:ComplexPortal.
DR GO; GO:1900232; P:negative regulation of single-species biofilm formation on inanimate substrate; IMP:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR DisProt; DP00776; -.
DR Gene3D; 1.10.287.1050; -; 1.
DR Gene3D; 4.10.430.10; -; 1.
DR InterPro; IPR027444; H-NS_C_dom.
DR InterPro; IPR037150; H-NS_C_dom_sf.
DR InterPro; IPR001801; Histone_HNS.
DR InterPro; IPR027454; Histone_HNS_N.
DR Pfam; PF00816; Histone_HNS; 1.
DR PIRSF; PIRSF002096; HnS; 1.
DR SMART; SM00528; HNS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Hydroxylation; Reference proteome; Repressor; RNA-binding;
KW Stress response; Transcription; Transcription regulation;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11790731,
FT ECO:0000269|PubMed:2020545, ECO:0000269|PubMed:2126011,
FT ECO:0000269|PubMed:6370250, ECO:0000269|PubMed:6395665,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841,
FT ECO:0000269|PubMed:9868784, ECO:0000269|Ref.16"
FT CHAIN 2..137
FT /note="DNA-binding protein H-NS"
FT /id="PRO_0000168503"
FT DNA_BIND 112..117
FT /evidence="ECO:0000250|UniProtKB:P0A1S2"
FT REGION 21..63
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:9398522"
FT REGION 92..137
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000269|PubMed:8913298"
FT COILED 22..49
FT /evidence="ECO:0000269|PubMed:12460581,
FT ECO:0000269|PubMed:12592399"
FT SITE 12
FT /note="Interacts with Hha"
FT /evidence="ECO:0000269|PubMed:21600204"
FT MOD_RES 121
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 2..69
FT /note="Missing: No longer complements a deletion mutant,
FT has no dominant-negative effects on wild-type protein, does
FT not oligomerize."
FT /evidence="ECO:0000269|PubMed:9398522"
FT MUTAGEN 2..20
FT /note="Missing: No longer complements a deletion mutant,
FT has dominant-negative effects on wild-type protein,
FT oligomerizes."
FT /evidence="ECO:0000269|PubMed:9398522"
FT MUTAGEN 6
FT /note="K->P: No effect on oligomerization of N-terminal
FT fragment 1-89."
FT /evidence="ECO:0000269|PubMed:12460581"
FT MUTAGEN 12..15
FT /note="RTLR->ERLA: Decreased DNA-binding, loss of
FT preference for curved DNA."
FT /evidence="ECO:0000269|PubMed:12592399"
FT MUTAGEN 12
FT /note="R->C: Derepression of proV and bgl expression,
FT normal DNA-binding, normal oligomerization."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 12
FT /note="R->H: Derepression of proV and bgl expression,
FT normal DNA-binding, normal oligomerization. Fragments 1-46
FT and 1-64 no longer bind Hha."
FT /evidence="ECO:0000269|PubMed:16650431,
FT ECO:0000269|PubMed:8913298"
FT MUTAGEN 12
FT /note="R->K: Abolishes the interaction with Hha."
FT /evidence="ECO:0000269|PubMed:21600204"
FT MUTAGEN 15
FT /note="R->C: Derepression of proV and bgl expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 15
FT /note="R->H: Derepression of proV and bgl expression.
FT Fragments 1-46 and 1-64 fold incorrectly but still bind
FT Hha."
FT /evidence="ECO:0000269|PubMed:16650431,
FT ECO:0000269|PubMed:8913298"
FT MUTAGEN 17
FT /note="Q->P: Abolishes oligomerization of N-terminal
FT fragment 1-89."
FT /evidence="ECO:0000269|PubMed:12460581"
FT MUTAGEN 26
FT /note="L->P: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 30
FT /note="L->A,K: Wild-type function."
FT /evidence="ECO:0000269|PubMed:9398522"
FT MUTAGEN 30
FT /note="L->D: Derepression of proV and partial derepression
FT of bgl epxression, does not dimerize, anomalous protein
FT mobility on gels."
FT /evidence="ECO:0000269|PubMed:9398522"
FT MUTAGEN 30
FT /note="L->P: Derepression of proV and bgl epxression, does
FT not dimerize, anomalous protein mobility on gels. Protein
FT localizes to nucleoid but no longer forms discreet compact
FT clusters."
FT /evidence="ECO:0000269|PubMed:21903814,
FT ECO:0000269|PubMed:9398522"
FT MUTAGEN 32
FT /note="K->Q: Loss of Hha binding by fragment 1-64, protein
FT folding is unaffected."
FT /evidence="ECO:0000269|PubMed:26085102"
FT MUTAGEN 53..55
FT /note="ERT->GRP: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 54
FT /note="R->C: Derepression of proV and bgl expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 64..137
FT /note="Missing: No longer complements a deletion mutant,
FT has dominant-negative effects on wild-type protein,
FT oligomerizes."
FT /evidence="ECO:0000269|PubMed:8755860,
FT ECO:0000269|PubMed:9398522"
FT MUTAGEN 90
FT /note="R->C,H: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 91
FT /note="A->T: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 92..137
FT /note="Missing: Derepression of proV expression, loss of
FT DNA-binding, increased oligomerization. No longer
FT complements a deletion mutant, has dominant-negative
FT effects on wild-type protein, oligomerizes."
FT /evidence="ECO:0000269|PubMed:8913298,
FT ECO:0000269|PubMed:9398522"
FT MUTAGEN 93
FT /note="R->C: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 94
FT /note="P->L,S: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 95
FT /note="A->T: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 96
FT /note="K->Q: Does not affect hydroxyisobutyrylation."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 97
FT /note="Y->C,H,S: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 110
FT /note="T->A: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 110
FT /note="T->I: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 111
FT /note="G->D,S: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 113
FT /note="G->D: Derepression of proV expression, decreased
FT DNA-binding but still prefers curved DNA, increased
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 113
FT /note="G->S: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 114
FT /note="R->C,H: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 115
FT /note="T->I: Derepression of proV expression."
FT /evidence="ECO:0000269|PubMed:8913298"
FT MUTAGEN 116
FT /note="P->S: Partial loss of repressor function. Protein
FT localizes to nucleoid but forms about 20-fold fewer
FT localization points."
FT /evidence="ECO:0000269|PubMed:21903814,
FT ECO:0000269|PubMed:8755860"
FT MUTAGEN 119
FT /note="I->T: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 121
FT /note="K->Q: No change in hydroxyisobutyrylation levels.
FT Almost loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 121
FT /note="K->R: Does not affect DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:34903851"
FT MUTAGEN 122..137
FT /note="AMDEQGKSLDDFLIKQ->KQWMRKVNPSTIS: Partial loss of
FT repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT MUTAGEN 133
FT /note="F->S: Partial loss of repressor function."
FT /evidence="ECO:0000269|PubMed:8755860"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:1LR1"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:1LR1"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1LR1"
FT HELIX 24..51
FT /evidence="ECO:0007829|PDB:1LR1"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1HNR"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1HNS"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:1HNS"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1HNS"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1HNR"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1HNR"
SQ SEQUENCE 137 AA; 15540 MW; E628184AC7C86F49 CRC64;
MSEALKILNN IRTLRAQARE CTLETLEEML EKLEVVVNER REEESAAAAE VEERTRKLQQ
YREMLIADGI DPNELLNSLA AVKSGTKAKR AQRPAKYSYV DENGETKTWT GQGRTPAVIK
KAMDEQGKSL DDFLIKQ
