FLIT_YERE8
ID FLIT_YERE8 Reviewed; 120 AA.
AC A1JSR8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=YE2526;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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: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; AM286415; CAL12569.1; -; Genomic_DNA.
DR RefSeq; WP_011816593.1; NC_008800.1.
DR RefSeq; YP_001006733.1; NC_008800.1.
DR PDB; 3NKZ; X-ray; 2.11 A; A/B/C/D=1-120.
DR PDBsum; 3NKZ; -.
DR AlphaFoldDB; A1JSR8; -.
DR SMR; A1JSR8; -.
DR STRING; 393305.YE2526; -.
DR EnsemblBacteria; CAL12569; CAL12569; YE2526.
DR KEGG; yen:YE2526; -.
DR PATRIC; fig|393305.7.peg.2683; -.
DR eggNOG; ENOG5032ZV7; Bacteria.
DR HOGENOM; CLU_155793_1_0_6; -.
DR OMA; DMEITYL; -.
DR Proteomes; UP000000642; 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..120
FT /note="Flagellar protein FliT"
FT /id="PRO_0000353895"
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 1..25
FT /evidence="ECO:0007829|PDB:3NKZ"
FT HELIX 32..53
FT /evidence="ECO:0007829|PDB:3NKZ"
FT HELIX 58..93
FT /evidence="ECO:0007829|PDB:3NKZ"
SQ SEQUENCE 120 AA; 13713 MW; 64BE3ABEF7A1A4D4 CRC64;
MERHQHLLSE YQQILTLSEQ MLVLATEGNW DALVDLEMTY LKAVESTANI TISSCSSLML
QDLLREKLRA ILDNEIEIKR LLQLRLDRLS DLVGQSTKQQ AVNNTYGQFP DHALLLGETQ
