ID   FLIT_ECOUT              Reviewed;         121 AA.
AC   Q1RAL4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=UTI89_C2127;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE07600.1; -; Genomic_DNA.
DR   RefSeq; WP_001057836.1; NC_007946.1.
DR   AlphaFoldDB; Q1RAL4; -.
DR   SMR; Q1RAL4; -.
DR   EnsemblBacteria; ABE07600; ABE07600; UTI89_C2127.
DR   KEGG; eci:UTI89_C2127; -.
DR   HOGENOM; CLU_155793_1_1_6; -.
DR   OMA; DMEITYL; -.
DR   Proteomes; UP000001952; 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_0000353880"
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;  13743 MW;  63ED8D4F5C5BB266 CRC64;
     MNNAPHLYFA WQQLVEKSQL MLRLATEEQW DELIASEMAY VNAVQEIAHL TEEVAPSTTM
     QEQLRPMLHL ILDNESKVKQ LLQIRMDELA KLVGQSSVQK SVLSAYGDQG GFVLAPQDNL
     F