FLHD_CUPPJ
ID FLHD_CUPPJ Reviewed; 105 AA.
AC Q46PI5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725}; OrderedLocusNames=Reut_B5604;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000091; AAZ64949.1; -; Genomic_DNA.
DR RefSeq; WP_011301712.1; NC_007348.1.
DR AlphaFoldDB; Q46PI5; -.
DR SMR; Q46PI5; -.
DR STRING; 264198.Reut_B5604; -.
DR EnsemblBacteria; AAZ64949; AAZ64949; Reut_B5604.
DR KEGG; reu:Reut_B5604; -.
DR eggNOG; ENOG5031P80; Bacteria.
DR HOGENOM; CLU_144160_1_0_4; -.
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 3: Inferred from homology;
KW Activator; Bacterial flagellum biogenesis; Cytoplasm; Disulfide bond;
KW DNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..105
FT /note="Flagellar transcriptional regulator FlhD"
FT /id="PRO_1000045886"
FT DISULFID 65
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00725"
SQ SEQUENCE 105 AA; 11872 MW; 2FC44C5A588C0CE8 CRC64;
MESSEVLQEI REVNLAYLLL AQRLVRENQV EAMFRLGVSK EIADILAKLT SAQLVKLAAS
NMVLCRFRFD DHALLSTLTH TAKNHDMQQM HAAILLARQP VESLN