ID   FLIT_SALAR              Reviewed;         122 AA.
AC   A9MML7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-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}; OrderedLocusNames=SARI_00975;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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; CP000880; ABX20886.1; -; Genomic_DNA.
DR   RefSeq; WP_000204901.1; NC_010067.1.
DR   AlphaFoldDB; A9MML7; -.
DR   SMR; A9MML7; -.
DR   STRING; 41514.SARI_00975; -.
DR   EnsemblBacteria; ABX20886; ABX20886; SARI_00975.
DR   KEGG; ses:SARI_00975; -.
DR   HOGENOM; CLU_155793_1_0_6; -.
DR   OMA; DMEITYL; -.
DR   OrthoDB; 2065730at2; -.
DR   Proteomes; UP000002084; 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..122
FT                   /note="Flagellar protein FliT"
FT                   /id="PRO_0000353887"
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   122 AA;  13732 MW;  7EA95E07CDC84B48 CRC64;
     MTSTVEFINR WQRIALLSQS LLELAQRGEW ELLLQQEVSY LQSIETVMEK QTPPGITRSI
     QDMVAGYIKQ TLDNEQRLKG LLQQRLDELS GLIGQSTRQK SLNNAYGRLS GMLLVPDAPG
     AS