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Protein

Flagellar transcriptional regulator FlhD

Gene

flhD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.4 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. bacterial-type flagellum assembly Source: InterPro
  2. positive regulation of transcription, DNA-templated Source: InterPro
  3. regulation of bacterial-type flagellum assembly Source: UniProtKB-HAMAP
  4. transcription, DNA-templated Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Bacterial flagellum biogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10320-MONOMER.
ECOL316407:JW1881-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flagellar transcriptional regulator FlhD
Gene namesi
Name:flhD
Synonyms:flbB
Ordered Locus Names:b1892, JW1881
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10320. flhD.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21H → A: Partial swarming phenotype. 1 Publication
Mutagenesisi28 – 281D → A: Partial swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi34 – 341F → A: Partial swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi35 – 351R → A: Partial swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi61 – 611N → A: Partial swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi82 – 821S → A: Partial swarming phenotype. Does not affect FlhD/FlhC complex formation, but affects DNA binding. 1 Publication
Mutagenesisi83 – 831R → A: Partial swarming phenotype. Does not affect FlhD/FlhC complex formation, but affects DNA binding. 1 Publication
Mutagenesisi84 – 841V → A: Partial swarming phenotype. Does not affect FlhD/FlhC complex formation, but affects DNA binding. 1 Publication
Mutagenesisi91 – 911H → A: Partial swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi92 – 921T → A: Non-swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi94 – 941I → A: Non-swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication
Mutagenesisi96 – 961L → A: Partial swarming phenotype. Affects FlhD/FlhC complex formation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 116116Flagellar transcriptional regulator FlhDPRO_0000182713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 – 65Interchain

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Expression is regulated by a large number of systems, including induction by quorum sensing via the two-component regulatory system QseB/QseC, induction by cAMP-CRP, repression by high osmolarity via OmpR and repression by H-NS.3 Publications

Gene expression databases

GenevestigatoriP0A8S9.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Forms a heterohexamer composed of two FlhC and four FlhD subunits. Each FlhC binds a FlhD dimer, forming a heterotrimer, and a hexamer assembles by dimerization of two heterotrimers.1 Publication

Protein-protein interaction databases

DIPiDIP-9646N.
IntActiP0A8S9. 14 interactions.
STRINGi511145.b1892.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2724Combined sources
Helixi29 – 368Combined sources
Helixi40 – 478Combined sources
Helixi51 – 588Combined sources
Beta strandi59 – 624Combined sources
Beta strandi64 – 685Combined sources
Helixi72 – 787Combined sources
Helixi83 – 919Combined sources
Helixi94 – 974Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8EX-ray1.80A/B1-116[»]
2AVUX-ray3.00A/B/C/D1-116[»]
4ES4X-ray2.90B/D/F/H1-116[»]
ProteinModelPortaliP0A8S9.
SMRiP0A8S9. Positions 3-106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8S9.

Family & Domainsi

Domaini

The C-terminal region contains a putative helix-turn-helix (HTH) motif, suggesting that this region may bind DNA.1 Publication

Sequence similaritiesi

Belongs to the FlhD family.Curated

Phylogenomic databases

eggNOGiNOG07455.
HOGENOMiHOG000254676.
KOiK02403.
OMAiETNQLIC.
OrthoDBiEOG64JFRM.

Family and domain databases

HAMAPiMF_00725. FlhD.
InterProiIPR023559. Flagellar_FlhD.
[Graphical view]
PfamiPF05247. FlhD. 1 hit.
[Graphical view]
ProDomiPD015582. Flagellar_transcriptional_act. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63592. SSF63592. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A8S9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHTSELLKHI YDINLSYLLL AQRLIVQDKA SAMFRLGINE EMATTLAALT
60 70 80 90 100
LPQMVKLAET NQLVCHFRFD SHQTITQLTQ DSRVDDLQQI HTGIMLSTRL
110
LNDVNQPEEA LRKKRA
Length:116
Mass (Da):13,316
Last modified:June 7, 2005 - v1
Checksum:i593287239E9A4C16
GO

Sequence cautioni

The sequence AAA23787.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA15713.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 13317 Da from positions 1 - 116. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19439 Genomic DNA. Translation: AAA23787.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74962.2.
AP009048 Genomic DNA. Translation: BAA15713.1. Different initiation.
PIRiA27735. XMECFB.
RefSeqiNP_416406.4. NC_000913.3.
YP_490154.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74962; AAC74962; b1892.
BAA15713; BAA15713; BAA15713.
GeneIDi12933247.
945442.
KEGGiecj:Y75_p1868.
eco:b1892.
PATRICi32119111. VBIEscCol129921_1973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19439 Genomic DNA. Translation: AAA23787.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74962.2.
AP009048 Genomic DNA. Translation: BAA15713.1. Different initiation.
PIRiA27735. XMECFB.
RefSeqiNP_416406.4. NC_000913.3.
YP_490154.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8EX-ray1.80A/B1-116[»]
2AVUX-ray3.00A/B/C/D1-116[»]
4ES4X-ray2.90B/D/F/H1-116[»]
ProteinModelPortaliP0A8S9.
SMRiP0A8S9. Positions 3-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9646N.
IntActiP0A8S9. 14 interactions.
STRINGi511145.b1892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74962; AAC74962; b1892.
BAA15713; BAA15713; BAA15713.
GeneIDi12933247.
945442.
KEGGiecj:Y75_p1868.
eco:b1892.
PATRICi32119111. VBIEscCol129921_1973.

Organism-specific databases

EchoBASEiEB0316.
EcoGeneiEG10320. flhD.

Phylogenomic databases

eggNOGiNOG07455.
HOGENOMiHOG000254676.
KOiK02403.
OMAiETNQLIC.
OrthoDBiEOG64JFRM.

Enzyme and pathway databases

BioCyciEcoCyc:EG10320-MONOMER.
ECOL316407:JW1881-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A8S9.
PROiP0A8S9.

Gene expression databases

GenevestigatoriP0A8S9.

Family and domain databases

HAMAPiMF_00725. FlhD.
InterProiIPR023559. Flagellar_FlhD.
[Graphical view]
PfamiPF05247. FlhD. 1 hit.
[Graphical view]
ProDomiPD015582. Flagellar_transcriptional_act. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63592. SSF63592. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Flagellar transcriptional activators FlbB and FlaI: gene sequences and 5' consensus sequences of operons under FlbB and FlaI control."
    Bartlett D.H., Frantz B.B., Matsumura P.
    J. Bacteriol. 170:1575-1581(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli flagellar class II operons."
    Liu X., Matsumura P.
    J. Bacteriol. 176:7345-7351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FLHC, DNA-BINDING.
    Strain: K12 / MC1000 / ATCC 39531.
  6. "Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR."
    Shin S., Park C.
    J. Bacteriol. 177:4696-4702(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12.
  7. "Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon."
    Soutourina O., Kolb A., Krin E., Laurent-Winter C., Rimsky S., Danchin A., Bertin P.
    J. Bacteriol. 181:7500-7508(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, INDUCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Extensive alanine scanning reveals protein-protein and protein-DNA interaction surfaces in the global regulator FlhD from Escherichia coli."
    Campos A., Matsumura P.
    Mol. Microbiol. 39:581-594(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FLHC, MUTAGENESIS OF HIS-2; ASP-28; PHE-34; ARG-35; ASN-61; SER-82; ARG-83; VAL-84; HIS-91; THR-92; ILE-94 AND LEU-96.
    Strain: K12 / YK410.
  9. "Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli."
    Sperandio V., Torres A.G., Kaper J.B.
    Mol. Microbiol. 43:809-821(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: K12.
  10. "Binding and transcriptional activation of non-flagellar genes by the Escherichia coli flagellar master regulator FlhD2C2."
    Stafford G.P., Ogi T., Hughes C.
    Microbiology 151:1779-1788(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
    Strain: K12 / MC1000 / ATCC 39531.
  11. "Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli."
    Pesavento C., Becker G., Sommerfeldt N., Possling A., Tschowri N., Mehlis A., Hengge R.
    Genes Dev. 22:2434-2446(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574 and K12 / W3110 / ATCC 27325 / DSM 5911.
  12. "Mutations in the flhD gene of Escherichia coli K-12 do not cause the reported effect on cell division."
    Siegele D.A., Bain S., Mao W.
    FEMS Microbiol. Lett. 309:94-99(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SHOWS THAT IT DOES NOT REGULATE CELL DIVISION.
    Strain: K12.
  13. "Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution."
    Campos A., Zhang R.G., Alkire R.W., Matsumura P., Westbrook E.M.
    Mol. Microbiol. 39:567-580(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-116, DOMAIN.
  14. "Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription."
    Wang S., Fleming R.T., Westbrook E.M., Matsumura P., McKay D.B.
    J. Mol. Biol. 355:798-808(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiFLHD_ECOLI
AccessioniPrimary (citable) accession number: P0A8S9
Secondary accession number(s): P11164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 7, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has been reported to be involved in cell division regulation, but it was later shown that this is not the case.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.