ID   FLIT_SALTI              Reviewed;         122 AA.
AC   P0A1N3; P26611;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN   OrderedLocusNames=STY2170, t0915;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL513382; CAD05710.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68593.1; -; Genomic_DNA.
DR   RefSeq; NP_456523.1; NC_003198.1.
DR   RefSeq; WP_000204899.1; NZ_WSUR01000004.1.
DR   PDB; 6CH2; X-ray; 2.70 A; D/E/F=1-122.
DR   PDBsum; 6CH2; -.
DR   AlphaFoldDB; P0A1N3; -.
DR   SMR; P0A1N3; -.
DR   STRING; 220341.16503203; -.
DR   EnsemblBacteria; AAO68593; AAO68593; t0915.
DR   KEGG; stt:t0915; -.
DR   KEGG; sty:STY2170; -.
DR   PATRIC; fig|220341.7.peg.2183; -.
DR   eggNOG; ENOG5032XUH; Bacteria.
DR   HOGENOM; CLU_155793_1_0_6; -.
DR   OMA; DMEITYL; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   1: Evidence at protein level;
KW   3D-structure; Bacterial flagellum biogenesis; Chaperone; Cytoplasm;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..122
FT                   /note="Flagellar protein FliT"
FT                   /id="PRO_0000180976"
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"
FT   HELIX           5..26
FT                   /evidence="ECO:0007829|PDB:6CH2"
FT   HELIX           30..49
FT                   /evidence="ECO:0007829|PDB:6CH2"
FT   HELIX           58..106
FT                   /evidence="ECO:0007829|PDB:6CH2"
SQ   SEQUENCE   122 AA;  13705 MW;  CF622E06DCD122AB CRC64;
     MTSTVEFINR WQRIALLSQS LLELAQRGEW DLLLQQEVSY LQSIETVMEK QTPPGITRSI
     QDMVAGYIKQ TLDNEQLLKG LLQQRLDELS SLIGQSTRQK SLNNAYGRLS GMLLVPDAPG
     AS