FLHD_ACISJ
ID FLHD_ACISJ Reviewed; 109 AA.
AC A1W9V0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=Ajs_2884;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00725}.
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:0000255|HAMAP-Rule:MF_00725}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00725}.
CC -!- DOMAIN: The C-terminal region contains a putative helix-turn-helix
CC (HTH) motif, suggesting that this region may bind DNA.
CC {ECO:0000255|HAMAP-Rule:MF_00725}.
CC -!- SIMILARITY: Belongs to the FlhD family. {ECO:0000255|HAMAP-
CC Rule:MF_00725}.
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DR EMBL; CP000539; ABM43025.1; -; Genomic_DNA.
DR RefSeq; WP_011806037.1; NC_008782.1.
DR AlphaFoldDB; A1W9V0; -.
DR SMR; A1W9V0; -.
DR STRING; 232721.Ajs_2884; -.
DR EnsemblBacteria; ABM43025; ABM43025; Ajs_2884.
DR KEGG; ajs:Ajs_2884; -.
DR eggNOG; ENOG5031P80; Bacteria.
DR HOGENOM; CLU_144160_1_0_4; -.
DR OMA; HNTPRKA; -.
DR Proteomes; UP000000645; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:1902208; P:regulation of bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Activator; Bacterial flagellum biogenesis; Cytoplasm; Disulfide bond;
KW DNA-binding; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..109
FT /note="Flagellar transcriptional regulator FlhD"
FT /id="PRO_0000406769"
FT DISULFID 65
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ SEQUENCE 109 AA; 12012 MW; 4C640D7D5E80D828 CRC64;
MTSEQLLAEI REANLTYLML AQTLIRQDKA EAVFRLGLNE EAADILASLS AAQVLKLASR
NTLLCSFRVD DELVWSLLTS HNTPRKAASE ATNTLHANIL MASRVSEVL