FLIT_SERP5
ID FLIT_SERP5 Reviewed; 122 AA.
AC A8GG04;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Flagellar protein FliT {ECO:0000255|HAMAP-Rule:MF_01180};
GN Name=fliT {ECO:0000255|HAMAP-Rule:MF_01180}; OrderedLocusNames=Spro_2943;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV42044.1; -; Genomic_DNA.
DR RefSeq; WP_012145665.1; NC_009832.1.
DR AlphaFoldDB; A8GG04; -.
DR SMR; A8GG04; -.
DR STRING; 399741.Spro_2943; -.
DR EnsemblBacteria; ABV42044; ABV42044; Spro_2943.
DR KEGG; spe:Spro_2943; -.
DR eggNOG; ENOG5032ZV7; Bacteria.
DR HOGENOM; CLU_155793_1_0_6; -.
DR OMA; DMEITYL; -.
DR OrthoDB; 2065730at2; -.
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_0000353891"
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; 13945 MW; 5562C84CBF3CAD44 CRC64;
MERQQQLLAA YQQIHSLSSQ MIALAQTERW EDLVELELAY VTAVESTAAF TGQAGPSMAL
QELLRNKLQQ ILDNETELKR LLQQRMDQLK ELIGQSTRQN VVNSTYGQFN DRALLLGEPQ
IR