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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

GO - Biological processi

  • bacterial-type flagellum assembly Source: InterPro
  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • positive regulation of transcription, DNA-templated Source: EcoCyc
  • regulation of bacterial-type flagellum assembly Source: UniProtKB-HAMAP
  • 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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10320. flhD.

Subcellular locationi

GO - Cellular componenti

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

Proteomic databases

PaxDbiP0A8S9.

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

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

BioGridi4262241. 7 interactions.
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

eggNOGiENOG4105GEH. Bacteria.
ENOG4111JRF. LUCA.
HOGENOMiHOG000254676.
KOiK02403.
OMAiREDKPMG.

Family and domain databases

HAMAPiMF_00725. FlhD. 1 hit.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA15713 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.
WP_001295647.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74962; AAC74962; b1892.
BAA15713; BAA15713; BAA15713.
GeneIDi945442.
KEGGiecj:JW1881.
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.
WP_001295647.1. NZ_LN832404.1.

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

BioGridi4262241. 7 interactions.
DIPiDIP-9646N.
IntActiP0A8S9. 14 interactions.
STRINGi511145.b1892.

Proteomic databases

PaxDbiP0A8S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74962; AAC74962; b1892.
BAA15713; BAA15713; BAA15713.
GeneIDi945442.
KEGGiecj:JW1881.
eco:b1892.
PATRICi32119111. VBIEscCol129921_1973.

Organism-specific databases

EchoBASEiEB0316.
EcoGeneiEG10320. flhD.

Phylogenomic databases

eggNOGiENOG4105GEH. Bacteria.
ENOG4111JRF. LUCA.
HOGENOMiHOG000254676.
KOiK02403.
OMAiREDKPMG.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A8S9.
PROiP0A8S9.

Family and domain databases

HAMAPiMF_00725. FlhD. 1 hit.
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...

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: September 7, 2016
This is version 94 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

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 one 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.