ID   FLIT_CITK8              Reviewed;         120 AA.
AC   A8AF95;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=CKO_01012;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV12158.1; -; Genomic_DNA.
DR   RefSeq; WP_012131914.1; NC_009792.1.
DR   AlphaFoldDB; A8AF95; -.
DR   SMR; A8AF95; -.
DR   STRING; 290338.CKO_01012; -.
DR   EnsemblBacteria; ABV12158; ABV12158; CKO_01012.
DR   GeneID; 45135174; -.
DR   KEGG; cko:CKO_01012; -.
DR   HOGENOM; CLU_155793_1_0_6; -.
DR   OMA; DMEITYL; -.
DR   OrthoDB; 2065730at2; -.
DR   Proteomes; UP000008148; 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; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..120
FT                   /note="Flagellar protein FliT"
FT                   /id="PRO_0000353872"
FT   REGION          1..50
FT                   /note="Required for homodimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01180"
FT   REGION          59..97
FT                   /note="FliD binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01180"
SQ   SEQUENCE   120 AA;  13569 MW;  32E7A4CB5B8BC420 CRC64;
     MTNFIPSLTD WHALHALSIT MLDLAHSGKW DELIEQEMNY VQLVEGIARN PISPGNTFLI
     NQAKEILNAV LRNEAELKTL LQHRMEELRQ LIDQTGKQQS VSTTYGNLAG NILFPSNLNQ