FLHD_ECOLI
ID FLHD_ECOLI Reviewed; 116 AA.
AC P0A8S9; P11164;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Flagellar transcriptional regulator FlhD;
GN Name=flhD; Synonyms=flbB; OrderedLocusNames=b1892, JW1881;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832369; DOI=10.1128/jb.170.4.1575-1581.1988;
RA Bartlett D.H., Frantz B.B., Matsumura P.;
RT "Flagellar transcriptional activators FlbB and FlaI: gene sequences and 5'
RT consensus sequences of operons under FlbB and FlaI control.";
RL J. Bacteriol. 170:1575-1581(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, INTERACTION WITH FLHC, AND DNA-BINDING.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=7961507; DOI=10.1128/jb.176.23.7345-7351.1994;
RA Liu X., Matsumura P.;
RT "The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli
RT flagellar class II operons.";
RL J. Bacteriol. 176:7345-7351(1994).
RN [6]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=7642497; DOI=10.1128/jb.177.16.4696-4702.1995;
RA Shin S., Park C.;
RT "Modulation of flagellar expression in Escherichia coli by acetyl phosphate
RT and the osmoregulator OmpR.";
RL J. Bacteriol. 177:4696-4702(1995).
RN [7]
RP MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10601207; DOI=10.1128/jb.181.24.7500-7508.1999;
RA Soutourina O., Kolb A., Krin E., Laurent-Winter C., Rimsky S., Danchin A.,
RA Bertin P.;
RT "Multiple control of flagellum biosynthesis in Escherichia coli: role of H-
RT NS protein and the cyclic AMP-catabolite activator protein complex in
RT transcription of the flhDC master operon.";
RL J. Bacteriol. 181:7500-7508(1999).
RN [8]
RP FUNCTION, INTERACTION WITH FLHC, AND MUTAGENESIS OF HIS-2; ASP-28; PHE-34;
RP ARG-35; ASN-61; SER-82; ARG-83; VAL-84; HIS-91; THR-92; ILE-94 AND LEU-96.
RC STRAIN=K12 / YK410;
RX PubMed=11169100; DOI=10.1046/j.1365-2958.2001.02248.x;
RA Campos A., Matsumura P.;
RT "Extensive alanine scanning reveals protein-protein and protein-DNA
RT interaction surfaces in the global regulator FlhD from Escherichia coli.";
RL Mol. Microbiol. 39:581-594(2001).
RN [9]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=11929534; DOI=10.1046/j.1365-2958.2002.02803.x;
RA Sperandio V., Torres A.G., Kaper J.B.;
RT "Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-
RT component regulatory system involved in the regulation of flagella and
RT motility by quorum sensing in E. coli.";
RL Mol. Microbiol. 43:809-821(2002).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=15941987; DOI=10.1099/mic.0.27879-0;
RA Stafford G.P., Ogi T., Hughes C.;
RT "Binding and transcriptional activation of non-flagellar genes by the
RT Escherichia coli flagellar master regulator FlhD2C2.";
RL Microbiology 151:1779-1788(2005).
RN [11]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574, and
RC K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=18765794; DOI=10.1101/gad.475808;
RA Pesavento C., Becker G., Sommerfeldt N., Possling A., Tschowri N.,
RA Mehlis A., Hengge R.;
RT "Inverse regulatory coordination of motility and curli-mediated adhesion in
RT Escherichia coli.";
RL Genes Dev. 22:2434-2446(2008).
RN [12]
RP SHOWS THAT IT DOES NOT REGULATE CELL DIVISION.
RC STRAIN=K12;
RX PubMed=20546312; DOI=10.1111/j.1574-6968.2010.02021.x;
RA Siegele D.A., Bain S., Mao W.;
RT "Mutations in the flhD gene of Escherichia coli K-12 do not cause the
RT reported effect on cell division.";
RL FEMS Microbiol. Lett. 309:94-99(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-116, AND DOMAIN.
RX PubMed=11169099; DOI=10.1046/j.1365-2958.2001.02247.x;
RA Campos A., Zhang R.G., Alkire R.W., Matsumura P., Westbrook E.M.;
RT "Crystal structure of the global regulator FlhD from Escherichia coli at
RT 1.8 A resolution.";
RL Mol. Microbiol. 39:567-580(2001).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=16337229; DOI=10.1016/j.jmb.2005.11.020;
RA Wang S., Fleming R.T., Westbrook E.M., Matsumura P., McKay D.B.;
RT "Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric
RT regulator of transcription.";
RL J. Mol. Biol. 355:798-808(2006).
CC -!- FUNCTION: Functions in complex with FlhC as a master transcriptional
CC regulator that regulates transcription of several flagellar and non-
CC flagellar operons by binding to their promoter region. Activates
CC expression of class 2 flagellar genes, including fliA, which is a
CC flagellum-specific sigma factor that turns on the class 3 genes. Also
CC regulates genes whose products function in a variety of physiological
CC pathways. {ECO:0000269|PubMed:11169100, ECO:0000269|PubMed:15941987,
CC ECO:0000269|PubMed:18765794, ECO:0000269|PubMed:7961507}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Forms a heterohexamer composed of
CC two FlhC and four FlhD subunits. Each FlhC binds a FlhD dimer, forming
CC a heterotrimer, and a hexamer assembles by dimerization of two
CC heterotrimers. {ECO:0000269|PubMed:16337229}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Expression is regulated by a large number of systems,
CC including induction by quorum sensing via the two-component regulatory
CC system QseB/QseC, induction by cAMP-CRP, repression by high osmolarity
CC via OmpR and repression by H-NS. {ECO:0000269|PubMed:10601207,
CC ECO:0000269|PubMed:11929534, ECO:0000269|PubMed:7642497}.
CC -!- DOMAIN: The C-terminal region contains a putative helix-turn-helix
CC (HTH) motif, suggesting that this region may bind DNA.
CC {ECO:0000269|PubMed:11169099}.
CC -!- MASS SPECTROMETRY: Mass=13317; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:10601207};
CC -!- MISCELLANEOUS: Has been reported to be involved in cell division
CC regulation, but it was later shown that this is not the case.
CC {ECO:0000305|PubMed:20546312}.
CC -!- SIMILARITY: Belongs to the FlhD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23787.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA15713.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M19439; AAA23787.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74962.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15713.1; ALT_INIT; Genomic_DNA.
DR PIR; A27735; XMECFB.
DR RefSeq; NP_416406.4; NC_000913.3.
DR RefSeq; WP_001295647.1; NZ_SSUW01000051.1.
DR PDB; 1G8E; X-ray; 1.80 A; A/B=1-116.
DR PDB; 2AVU; X-ray; 3.00 A; A/B/C/D=1-116.
DR PDB; 4ES4; X-ray; 2.90 A; B/D/F/H=1-116.
DR PDBsum; 1G8E; -.
DR PDBsum; 2AVU; -.
DR PDBsum; 4ES4; -.
DR AlphaFoldDB; P0A8S9; -.
DR SMR; P0A8S9; -.
DR BioGRID; 4262241; 7.
DR ComplexPortal; CPX-2508; FlhDC transcriptional regulation complex.
DR DIP; DIP-9646N; -.
DR IntAct; P0A8S9; 15.
DR STRING; 511145.b1892; -.
DR PaxDb; P0A8S9; -.
DR PRIDE; P0A8S9; -.
DR EnsemblBacteria; AAC74962; AAC74962; b1892.
DR EnsemblBacteria; BAA15713; BAA15713; BAA15713.
DR GeneID; 58462231; -.
DR GeneID; 945442; -.
DR KEGG; ecj:JW1881; -.
DR KEGG; eco:b1892; -.
DR PATRIC; fig|1411691.4.peg.355; -.
DR EchoBASE; EB0316; -.
DR eggNOG; ENOG5031P80; Bacteria.
DR HOGENOM; CLU_144160_0_0_6; -.
DR OMA; REDKPMG; -.
DR PhylomeDB; P0A8S9; -.
DR BioCyc; EcoCyc:EG10320-MON; -.
DR EvolutionaryTrace; P0A8S9; -.
DR PRO; PR:P0A8S9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:1902210; P:positive regulation of bacterial-type flagellum assembly; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR DisProt; DP02700; -.
DR Gene3D; 1.10.4000.10; -; 1.
DR HAMAP; MF_00725; FlhD; 1.
DR InterPro; IPR023559; Flagellar_FlhD.
DR InterPro; IPR036194; FlhD_sf.
DR Pfam; PF05247; FlhD; 1.
DR SUPFAM; SSF63592; SSF63592; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Bacterial flagellum biogenesis; Cytoplasm;
KW Disulfide bond; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..116
FT /note="Flagellar transcriptional regulator FlhD"
FT /id="PRO_0000182713"
FT DISULFID 65
FT /note="Interchain"
FT MUTAGEN 2
FT /note="H->A: Partial swarming phenotype."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 28
FT /note="D->A: Partial swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 34
FT /note="F->A: Partial swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 35
FT /note="R->A: Partial swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 61
FT /note="N->A: Partial swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 82
FT /note="S->A: Partial swarming phenotype. Does not affect
FT FlhD/FlhC complex formation, but affects DNA binding."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 83
FT /note="R->A: Partial swarming phenotype. Does not affect
FT FlhD/FlhC complex formation, but affects DNA binding."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 84
FT /note="V->A: Partial swarming phenotype. Does not affect
FT FlhD/FlhC complex formation, but affects DNA binding."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 91
FT /note="H->A: Partial swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 92
FT /note="T->A: Non-swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 94
FT /note="I->A: Non-swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT MUTAGEN 96
FT /note="L->A: Partial swarming phenotype. Affects FlhD/FlhC
FT complex formation."
FT /evidence="ECO:0000269|PubMed:11169100"
FT HELIX 4..27
FT /evidence="ECO:0007829|PDB:1G8E"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1G8E"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:1G8E"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1G8E"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1G8E"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1G8E"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:1G8E"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1G8E"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1G8E"
SQ SEQUENCE 116 AA; 13316 MW; 593287239E9A4C16 CRC64;
MHTSELLKHI YDINLSYLLL AQRLIVQDKA SAMFRLGINE EMATTLAALT LPQMVKLAET
NQLVCHFRFD SHQTITQLTQ DSRVDDLQQI HTGIMLSTRL LNDVNQPEEA LRKKRA
