ID   FLIT_YERPB              Reviewed;         120 AA.
AC   B2K177;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=YPTS_1839;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) 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; CP001048; ACC88806.1; -; Genomic_DNA.
DR   RefSeq; WP_011192185.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K177; -.
DR   SMR; B2K177; -.
DR   GeneID; 66841855; -.
DR   KEGG; ypb:YPTS_1839; -.
DR   PATRIC; fig|502801.10.peg.1219; -.
DR   OMA; DMEITYL; -.
DR   BioCyc; YPSE502801:YPTS_RS09370-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..120
FT                   /note="Flagellar protein FliT"
FT                   /id="PRO_0000353902"
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   120 AA;  13869 MW;  4CB2E4ACA1D79C93 CRC64;
     MERHQHLLSE YQQILTLSEQ MLMLATVENW DALVDLEMAY LKAVENTANI TISSCSSPVL
     QELLRQKLRS ILENEIEIKR LLQRRLDKLS ELVGQSTRQQ AVNRTYGQFP DQALLLGETQ