FLIT_YERPA
ID FLIT_YERPA Reviewed; 120 AA.
AC Q1C8P0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=YPA_1215;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(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; CP000308; ABG13182.1; -; Genomic_DNA.
DR PIR; AD0224; AD0224.
DR RefSeq; WP_002211148.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C8P0; -.
DR SMR; Q1C8P0; -.
DR EnsemblBacteria; ABG13182; ABG13182; YPA_1215.
DR GeneID; 57976742; -.
DR KEGG; ypa:YPA_1215; -.
DR OMA; DMEITYL; -.
DR Proteomes; UP000001971; 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..120
FT /note="Flagellar protein FliT"
FT /id="PRO_0000353899"
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 120 AA; 13912 MW; 48B74413BE772789 CRC64;
MERHQHLLSE YQQILTLSEQ MLMLATVENW NALVDLEMTY LKAVENTANI TISSCTSPVL
QELLRQKLRS ILENEIEIKR LLQRRLDKLS ELVGQSTRQQ AVNRTYGQFP DQALLLGETQ