ID   FLHD_PROMI              Reviewed;         116 AA.
AC   O34201;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Flagellar transcriptional regulator FlhD;
GN   Name=flhD;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=U6450;
RX   PubMed=9287017; DOI=10.1128/jb.179.17.5585-5588.1997;
RA   Furness R.B., Fraser G.M., Hay N.A., Hughes C.;
RT   "Negative feedback from a Proteus class II flagellum export defect to the
RT   flhDC master operon controlling cell division and flagellum assembly.";
RL   J. Bacteriol. 179:5585-5588(1997).
RN   [2]
RP   FUNCTION, INTERACTION WITH FLHC, AND DNA-BINDING.
RC   STRAIN=U6450;
RX   PubMed=12144778; DOI=10.1016/s0022-2836(02)00600-9;
RA   Claret L., Hughes C.;
RT   "Interaction of the atypical prokaryotic transcription activator FlhD2C2
RT   with early promoters of the flagellar gene hierarchy.";
RL   J. Mol. Biol. 321:185-199(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:0000269|PubMed:12144778}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal region contains a putative helix-turn-helix
CC       (HTH) motif, suggesting that this region may bind DNA. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlhD family. {ECO:0000305}.
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DR   EMBL; U96964; AAB69767.1; -; Genomic_DNA.
DR   RefSeq; WP_004243568.1; NZ_WURR01000001.1.
DR   AlphaFoldDB; O34201; -.
DR   SMR; O34201; -.
DR   STRING; 584.AOUC001_07210; -.
DR   GeneID; 6801014; -.
DR   OMA; REDKPMG; -.
DR   OrthoDB; 2022460at2; -.
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   1: Evidence at protein level;
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_0000182721"
FT   DISULFID        65
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   116 AA;  13251 MW;  AA903B8CF17C6A5F CRC64;
     MSTVELLKHI YDINLSYLLL AQRLINQEKA SAMFRLGISD SMADALKELT LPQLVKLAET
     NQLICNFRFE DSETIEQLTK ESRVDDLQQI HTGILLSSNL FRQLSEHDTS ATKKRA