FLIT_ECODH
ID FLIT_ECODH Reviewed; 121 AA.
AC B1X683;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN OrderedLocusNames=ECDH10B_2067;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- FUNCTION: Dual-function protein that regulates the transcription of
CC class 2 flagellar operons and that also acts as an export chaperone for
CC the filament-capping protein FliD. As a transcriptional regulator, acts
CC as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the
CC binding of the FlhC/FlhD complex to class 2 promoters, resulting in
CC decreased expression of class 2 flagellar operons. As a chaperone,
CC effects FliD transition to the membrane by preventing its premature
CC polymerization, and by directing it to the export apparatus.
CC {ECO:0000255|HAMAP-Rule:MF_01180}.
CC -!- SUBUNIT: Homodimer. Interacts with FliD and FlhC. {ECO:0000255|HAMAP-
CC Rule:MF_01180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_01180}.
CC -!- SIMILARITY: Belongs to the FliT family. {ECO:0000255|HAMAP-
CC Rule:MF_01180}.
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DR EMBL; CP000948; ACB03115.1; -; Genomic_DNA.
DR RefSeq; WP_001015033.1; NC_010473.1.
DR AlphaFoldDB; B1X683; -.
DR SMR; B1X683; -.
DR KEGG; ecd:ECDH10B_2067; -.
DR HOGENOM; CLU_155793_1_1_6; -.
DR OMA; DMEITYL; -.
DR BioCyc; ECOL316385:ECDH10B_RS10585-MON; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR GO; GO:1902209; P:negative regulation of bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01180; FliT; 1.
DR InterPro; IPR008622; FliT.
DR Pfam; PF05400; FliT; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis; Chaperone; Cytoplasm; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..121
FT /note="Flagellar protein FliT"
FT /id="PRO_0000353878"
FT REGION 1..50
FT /note="Required for homodimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01180"
FT REGION 60..98
FT /note="FliD binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01180"
SQ SEQUENCE 121 AA; 13829 MW; 5FED8A383B8A1CF8 CRC64;
MNHAPHLYFA WQQLVEKSQL MLRLATEEQW DELIASEMAY VNAVQEIAHL TEEVDPSTTM
QEQLRPMLRL ILDNESKVKQ LLQIRMDELA KLVGQSSVQK SVLSAYGDQG GFVLAPQDNL
F