FLHD_YERPB
ID FLHD_YERPB Reviewed; 116 AA.
AC B2K6E0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=YPTS_2488;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC89449.1; -; Genomic_DNA.
DR RefSeq; WP_011192574.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K6E0; -.
DR SMR; B2K6E0; -.
DR GeneID; 66841159; -.
DR KEGG; ypb:YPTS_2488; -.
DR PATRIC; fig|502801.10.peg.1900; -.
DR OMA; REDKPMG; -.
DR BioCyc; YPSE502801:YPTS_RS12565-MON; -.
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_1000132696"
FT DISULFID 65
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ SEQUENCE 116 AA; 13235 MW; D942232879D1CF8F CRC64;
MSTSELLKHI YDINLSYLLL AQRLINDEKA SAMFRLGITD TMADALSQLT LPQMVKLAET
NQLVCHFRFS DHNTIHHLTK ESRVDDLQQI HTGILLSSHL LHELSLKDDS TPKKRA