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FLHD_SALSV
ID   FLHD_SALSV              Reviewed;         113 AA.
AC   B4TYV0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN   Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=SeSA_A2081;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001127; ACF92662.1; -; Genomic_DNA.
DR   RefSeq; WP_001518146.1; NC_011094.1.
DR   AlphaFoldDB; B4TYV0; -.
DR   SMR; B4TYV0; -.
DR   EnsemblBacteria; ACF92662; ACF92662; SeSA_A2081.
DR   KEGG; sew:SeSA_A2081; -.
DR   HOGENOM; CLU_144160_0_0_6; -.
DR   OMA; REDKPMG; -.
DR   Proteomes; UP000001865; 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..113
FT                   /note="Flagellar transcriptional regulator FlhD"
FT                   /id="PRO_1000132695"
FT   DISULFID        65
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ   SEQUENCE   113 AA;  13006 MW;  58327B10C1E385D9 CRC64;
     MHTSELLKHI YDINLSYLLL AQRLIVQDKA SAMFRLGINE EMANTLGALT LPQMVKLAET
     NQLVCHFRFD DHQTITRLTQ DSRVDDLQQI HTGIMLSTRL LNEVDDTARK KRA
 
 
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