ID   FLIW_CAMJE              Reviewed;         129 AA.
AC   Q0P9H9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Flagellar assembly factor FliW {ECO:0000255|HAMAP-Rule:MF_01185};
GN   Name=fliW {ECO:0000255|HAMAP-Rule:MF_01185}; OrderedLocusNames=Cj1075;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
RN   [2]
RP   ROLE IN MOTILITY AND FLAGELLIN BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=480;
RX   PubMed=11895937; DOI=10.1128/iai.70.4.1761-1771.2002;
RA   Golden N.J., Acheson D.W.K.;
RT   "Identification of motility and autoagglutination Campylobacter jejuni
RT   mutants by random transposon mutagenesis.";
RL   Infect. Immun. 70:1761-1771(2002).
RN   [3]
RP   FUNCTION, INTERACTION WITH CSRA AND FLAA, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=27229370; DOI=10.1038/ncomms11667;
RA   Dugar G., Svensson S.L., Bischler T., Waeldchen S., Reinhardt R., Sauer M.,
RA   Sharma C.M.;
RT   "The CsrA-FliW network controls polar localization of the dual-function
RT   flagellin mRNA in Campylobacter jejuni.";
RL   Nat. Commun. 7:11667-11667(2016).
CC   -!- FUNCTION: Acts as an anti-CsrA protein, binds CsrA and prevents it from
CC       repressing translation of its target genes, one of which is flagellin.
CC       Binds to flagellin and participates in the assembly of the flagellum
CC       (Probable). Antagonizes CsrA-mediated translational repression of flaA
CC       in a promoter-independent manner, leading to expression of FlaA and
CC       probably other flagellar genes. Binds to FlaA, which releases CsrA to
CC       repress translation of flaA mRNA. Also has a negative effect on flaA
CC       transcription, and influences the localization of flaA mRNA to the
CC       poles of short, probably elongating, cells.
CC       {ECO:0000269|PubMed:27229370, ECO:0000305|PubMed:11895937}.
CC   -!- SUBUNIT: Interacts with translational regulator CsrA and flagellin A
CC       (flaA) (PubMed:27229370). {ECO:0000269|PubMed:27229370}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185}.
CC   -!- DISRUPTION PHENOTYPE: No longer autoagglutinates, loss of motility and
CC       decreased ability to invade human cell line (PubMed:11895937).
CC       Significantly decreased translation of flagellin A, 2-fold increase in
CC       flaA mRNA levels. Has 1 short flagella, the average swimming distance
CC       decreases about 30%. The mRNA for flaA is no longer localized to the
CC       cell poles in short, probably elongating, cells. A double csrA-fliW
CC       deletion expresses the same amount of flagellin A as the csrA deletion,
CC       has 2 wild-type length flagella, a wild-type swimming distance and
CC       restored localization of flaA mRNA to the poles of short, probably
CC       elongating, cells. {ECO:0000269|PubMed:11895937,
CC       ECO:0000269|PubMed:27229370}.
CC   -!- SIMILARITY: Belongs to the FliW family. {ECO:0000255|HAMAP-
CC       Rule:MF_01185}.
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DR   EMBL; AL111168; CAL35192.1; -; Genomic_DNA.
DR   PIR; F81310; F81310.
DR   RefSeq; WP_002852982.1; NC_002163.1.
DR   RefSeq; YP_002344468.1; NC_002163.1.
DR   AlphaFoldDB; Q0P9H9; -.
DR   SMR; Q0P9H9; -.
DR   IntAct; Q0P9H9; 14.
DR   STRING; 192222.Cj1075; -.
DR   PaxDb; Q0P9H9; -.
DR   PRIDE; Q0P9H9; -.
DR   EnsemblBacteria; CAL35192; CAL35192; Cj1075.
DR   GeneID; 905366; -.
DR   KEGG; cje:Cj1075; -.
DR   PATRIC; fig|192222.6.peg.1057; -.
DR   eggNOG; COG1699; Bacteria.
DR   HOGENOM; CLU_112356_2_0_7; -.
DR   OMA; TIHKMHL; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.290.10; -; 1.
DR   HAMAP; MF_01185; FliW; 1.
DR   InterPro; IPR003775; Flagellar_assembly_factor_FliW.
DR   InterPro; IPR024046; Flagellar_assmbl_FliW_dom_sf.
DR   PANTHER; PTHR39190; PTHR39190; 1.
DR   Pfam; PF02623; FliW; 1.
DR   SUPFAM; SSF141457; SSF141457; 1.
PE   1: Evidence at protein level;
KW   Bacterial flagellum biogenesis; Chaperone; Cytoplasm; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..129
FT                   /note="Flagellar assembly factor FliW"
FT                   /id="PRO_0000272975"
SQ   SEQUENCE   129 AA;  14844 MW;  B16779B934EDEF31 CRC64;
     MTLAVKCPIL GFEETKNMEF STIDEVFVRL KSLDGKDFSF VLINPYLIRP DYEFDIPTYY
     QELLSLTPES NMKIFNIVAI AKSIEESTVN FLAPVVINLD NNTMVQVILD TVNYPDFFQA
     DQIANYIKK