FLHD_ECO24
ID FLHD_ECO24 Reviewed; 116 AA.
AC A7ZN19;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Flagellar transcriptional regulator FlhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN Name=flhD {ECO:0000255|HAMAP-Rule:MF_00725};
GN OrderedLocusNames=EcE24377A_2125;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
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; CP000800; ABV20712.1; -; Genomic_DNA.
DR RefSeq; WP_001295647.1; NC_009801.1.
DR AlphaFoldDB; A7ZN19; -.
DR SMR; A7ZN19; -.
DR EnsemblBacteria; ABV20712; ABV20712; EcE24377A_2125.
DR GeneID; 58462231; -.
DR KEGG; ecw:EcE24377A_2125; -.
DR HOGENOM; CLU_144160_0_0_6; -.
DR OMA; REDKPMG; -.
DR Proteomes; UP000001122; 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_1000062097"
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