ID   FLHD_ECOK1              Reviewed;         119 AA.
AC   A1AC51;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN   Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=Ecok1_17470;
GN   ORFNames=APECO1_940;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1AC51; -.
DR   SMR; A1AC51; -.
DR   EnsemblBacteria; ABJ01241; ABJ01241; APECO1_940.
DR   KEGG; ecv:APECO1_940; -.
DR   HOGENOM; CLU_144160_0_0_6; -.
DR   OMA; REDKPMG; -.
DR   Proteomes; UP000008216; 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; Transcription; Transcription regulation.
FT   CHAIN           1..119
FT                   /note="Flagellar transcriptional regulator FlhD"
FT                   /id="PRO_1000062099"
FT   DISULFID        68
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ   SEQUENCE   119 AA;  13618 MW;  8432CE64E49177B9 CRC64;
     MGIMHTSELL KHIYDINLSY LLLAQRLIVQ DKASAMFRLG INEEMATTLA ALTLPQMVKL
     AETNQLVCHF RFDSHQTITQ LTQDSRVDDL QQIHTGIMLS TRLLNDVNQP EEALRKKRA