ID   FLIT_ECOSM              Reviewed;         121 AA.
AC   B1LQS9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   OrderedLocusNames=EcSMS35_1255;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(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; CP000970; ACB19117.1; -; Genomic_DNA.
DR   RefSeq; WP_001015024.1; NC_010498.1.
DR   AlphaFoldDB; B1LQS9; -.
DR   SMR; B1LQS9; -.
DR   EnsemblBacteria; ACB19117; ACB19117; EcSMS35_1255.
DR   KEGG; ecm:EcSMS35_1255; -.
DR   HOGENOM; CLU_155793_1_1_6; -.
DR   OMA; DMEITYL; -.
DR   Proteomes; UP000007011; Chromosome.
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_0000353879"
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;  13783 MW;  809D8A2AB91A0E7A CRC64;
     MNHAPHLYFA WQQLVEKSQL MLRLATEEQW DELIASEMAY VNAVQEIAHL TEEIDPSTTM
     QEQLRPMLRL ILDNESKVKQ LLQIRMDELA KLVGQSSVQK SVLSAYGDQG GFVLAPQDNL
     S