ID   FLHD_WIGBR              Reviewed;         114 AA.
AC   Q8D3H1;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN   Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=WIGBR0300;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24176.1; -; Genomic_DNA.
DR   RefSeq; WP_011069834.1; NC_004344.2.
DR   AlphaFoldDB; Q8D3H1; -.
DR   SMR; Q8D3H1; -.
DR   STRING; 36870.25165985; -.
DR   EnsemblBacteria; BAC24176; BAC24176; BAC24176.
DR   KEGG; wbr:flhD; -.
DR   eggNOG; ENOG5031P80; Bacteria.
DR   HOGENOM; CLU_144160_1_0_6; -.
DR   OMA; HNTPRKA; -.
DR   OrthoDB; 2022460at2; -.
DR   Proteomes; UP000000562; 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..114
FT                   /note="Flagellar transcriptional regulator FlhD"
FT                   /id="PRO_0000182727"
FT   DISULFID        65
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ   SEQUENCE   114 AA;  12965 MW;  2987436090C9FE09 CRC64;
     MSNDNILKNI HEINLSYLLL AQELIKQDKK VASFRLGVCE DTLNKISKLS LSELIKLGAI
     NQLICLLRLD DEKVINCLTR ESRVDELQQV HTGIMLSTQL LRSHKSNSNH ALKE