ID   FLHD_ECOHS              Reviewed;         116 AA.
AC   A8A195;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN   Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=EcHS_A1988;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV06299.1; -; Genomic_DNA.
DR   RefSeq; WP_001295647.1; NC_009800.1.
DR   AlphaFoldDB; A8A195; -.
DR   SMR; A8A195; -.
DR   GeneID; 58462231; -.
DR   KEGG; ecx:EcHS_A1988; -.
DR   HOGENOM; CLU_144160_0_0_6; -.
DR   OMA; REDKPMG; -.
DR   Proteomes; UP000001123; 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..116
FT                   /note="Flagellar transcriptional regulator FlhD"
FT                   /id="PRO_1000062098"
FT   DISULFID        65
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ   SEQUENCE   116 AA;  13316 MW;  593287239E9A4C16 CRC64;
     MHTSELLKHI YDINLSYLLL AQRLIVQDKA SAMFRLGINE EMATTLAALT LPQMVKLAET
     NQLVCHFRFD SHQTITQLTQ DSRVDDLQQI HTGIMLSTRL LNDVNQPEEA LRKKRA