FLIT_SALEP
ID FLIT_SALEP Reviewed; 122 AA.
AC B5R0Z6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=SEN1046;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(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; AM933172; CAR32631.1; -; Genomic_DNA.
DR RefSeq; WP_000204899.1; NC_011294.1.
DR AlphaFoldDB; B5R0Z6; -.
DR SMR; B5R0Z6; -.
DR KEGG; set:SEN1046; -.
DR HOGENOM; CLU_155793_1_0_6; -.
DR OMA; DMEITYL; -.
DR Proteomes; UP000000613; 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..122
FT /note="Flagellar protein FliT"
FT /id="PRO_1000138182"
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; 13705 MW; CF622E06DCD122AB CRC64;
MTSTVEFINR WQRIALLSQS LLELAQRGEW DLLLQQEVSY LQSIETVMEK QTPPGITRSI
QDMVAGYIKQ TLDNEQLLKG LLQQRLDELS SLIGQSTRQK SLNNAYGRLS GMLLVPDAPG
AS