FLIT_SALTY
ID FLIT_SALTY Reviewed; 122 AA.
AC P0A1N2; P26611;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Flagellar protein FliT;
GN Name=fliT; OrderedLocusNames=STM1962;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SJW1103;
RX PubMed=1527488; DOI=10.1099/00221287-138-6-1051;
RA Kawagishi I., Mueller V., Williams A.W., Irikura V.M., Macnab R.M.;
RT "Subdivision of flagellar region III of the Escherichia coli and Salmonella
RT typhimurium chromosomes and identification of two additional flagellar
RT genes.";
RL J. Gen. Microbiol. 138:1051-1065(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION IN THE REGULATION OF THE FLAGELLAR REGULON.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=10791024; DOI=10.1266/ggs.74.287;
RA Kutsukake K., Ikebe T., Yamamoto S.;
RT "Two novel regulatory genes, fliT and fliZ, in the flagellar regulon of
RT Salmonella.";
RL Genes Genet. Syst. 74:287-292(1999).
RN [4]
RP FUNCTION AS A CHAPERONE, AND INTERACTION WITH FLID.
RC STRAIN=SJW1103;
RX PubMed=10320579; DOI=10.1046/j.1365-2958.1999.01372.x;
RA Fraser G.M., Bennett J.C., Hughes C.;
RT "Substrate-specific binding of hook-associated proteins by FlgN and FliT,
RT putative chaperones for flagellum assembly.";
RL Mol. Microbiol. 32:569-580(1999).
RN [5]
RP FUNCTION AS A CHAPERONE, SUBUNIT, AND INTERACTION WITH FLID.
RC STRAIN=SJW1103;
RX PubMed=11169117; DOI=10.1046/j.1365-2958.2001.02268.x;
RA Bennett J.C., Thomas J., Fraser G.M., Hughes C.;
RT "Substrate complexes and domain organization of the Salmonella flagellar
RT export chaperones FlgN and FliT.";
RL Mol. Microbiol. 39:781-791(2001).
RN [6]
RP FUNCTION AS A TRANSCRIPTIONAL REGULATOR OF THE FLAGELLAR REGULON.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=16952964; DOI=10.1128/jb.00799-06;
RA Yamamoto S., Kutsukake K.;
RT "FliT acts as an anti-FlhD2C2 factor in the transcriptional control of the
RT flagellar regulon in Salmonella enterica serovar typhimurium.";
RL J. Bacteriol. 188:6703-6708(2006).
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:0000269|PubMed:10320579, ECO:0000269|PubMed:10791024,
CC ECO:0000269|PubMed:11169117, ECO:0000269|PubMed:16952964}.
CC -!- SUBUNIT: Homodimer. Interacts with FliD and FlhC.
CC {ECO:0000269|PubMed:10320579, ECO:0000269|PubMed:11169117}.
CC -!- INTERACTION:
CC P0A1N2; P06179: fliC; NbExp=2; IntAct=EBI-15610664, EBI-2011501;
CC P0A1N2; P16328: fliD; NbExp=4; IntAct=EBI-15610664, EBI-15850928;
CC P0A1N2; P26465: fliI; NbExp=2; IntAct=EBI-15610664, EBI-6515439;
CC P0A1N2; P0A1K1: fliJ; NbExp=6; IntAct=EBI-15610664, EBI-6410293;
CC P0A1N2; P0A1N2: fliT; NbExp=3; IntAct=EBI-15610664, EBI-15610664;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- SIMILARITY: Belongs to the FliT family. {ECO:0000305}.
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DR EMBL; M85241; AAA27078.1; -; Genomic_DNA.
DR EMBL; L01643; AAA27109.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20874.1; -; Genomic_DNA.
DR RefSeq; NP_460915.1; NC_003197.2.
DR RefSeq; WP_000204899.1; NC_003197.2.
DR PDB; 3A7M; X-ray; 3.20 A; A/B=1-122.
DR PDB; 5GNA; X-ray; 2.30 A; A=1-94.
DR PDB; 5KP0; NMR; -; A=1-95.
DR PDB; 5KRW; NMR; -; A=1-95.
DR PDB; 5KS6; NMR; -; A=1-122.
DR PDBsum; 3A7M; -.
DR PDBsum; 5GNA; -.
DR PDBsum; 5KP0; -.
DR PDBsum; 5KRW; -.
DR PDBsum; 5KS6; -.
DR AlphaFoldDB; P0A1N2; -.
DR SMR; P0A1N2; -.
DR DIP; DIP-60504N; -.
DR IntAct; P0A1N2; 5.
DR STRING; 99287.STM1962; -.
DR PaxDb; P0A1N2; -.
DR EnsemblBacteria; AAL20874; AAL20874; STM1962.
DR GeneID; 1253483; -.
DR KEGG; stm:STM1962; -.
DR PATRIC; fig|99287.12.peg.2078; -.
DR HOGENOM; CLU_155793_1_0_6; -.
DR OMA; DMEITYL; -.
DR PhylomeDB; P0A1N2; -.
DR BioCyc; SENT99287:STM1962-MON; -.
DR EvolutionaryTrace; P0A1N2; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..122
FT /note="Flagellar protein FliT"
FT /id="PRO_0000180977"
FT REGION 1..50
FT /note="Required for homodimerization"
FT REGION 60..98
FT /note="FliD binding"
FT HELIX 1..26
FT /evidence="ECO:0007829|PDB:5GNA"
FT HELIX 30..49
FT /evidence="ECO:0007829|PDB:5GNA"
FT HELIX 58..93
FT /evidence="ECO:0007829|PDB:5GNA"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:3A7M"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5KS6"
SQ SEQUENCE 122 AA; 13705 MW; CF622E06DCD122AB CRC64;
MTSTVEFINR WQRIALLSQS LLELAQRGEW DLLLQQEVSY LQSIETVMEK QTPPGITRSI
QDMVAGYIKQ TLDNEQLLKG LLQQRLDELS SLIGQSTRQK SLNNAYGRLS GMLLVPDAPG
AS
