FLIW_BACSU
ID FLIW_BACSU Reviewed; 143 AA.
AC P96503; Q795D3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Flagellar assembly factor FliW {ECO:0000255|HAMAP-Rule:MF_01185, ECO:0000303|PubMed:16936039};
GN Name=fliW {ECO:0000255|HAMAP-Rule:MF_01185, ECO:0000303|PubMed:16936039};
GN Synonyms=yviF; OrderedLocusNames=BSU35380;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969505; DOI=10.1099/13500872-142-11-3079;
RA Soldo B., Lazarevic V., Mauel C., Karamata D.;
RT "Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis
RT chromosome.";
RL Microbiology 142:3079-3088(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN FLAGELLAR ASSEMBLY, INTERACTION WITH FLAGELLIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16936039; DOI=10.1128/jb.00820-06;
RA Titz B., Rajagopala S.V., Ester C., Haeuser R., Uetz P.;
RT "Novel conserved assembly factor of the bacterial flagellum.";
RL J. Bacteriol. 188:7700-7706(2006).
RN [4]
RP INDUCTION.
RC STRAIN=168, and 1A96;
RX PubMed=17555441; DOI=10.1111/j.1365-2958.2007.05765.x;
RA Yakhnin H., Pandit P., Petty T.J., Baker C.S., Romeo T., Babitzke P.;
RT "CsrA of Bacillus subtilis regulates translation initiation of the gene
RT encoding the flagellin protein (hag) by blocking ribosome binding.";
RL Mol. Microbiol. 64:1605-1620(2007).
RN [5]
RP FUNCTION, INTERACTION WITH CSRA, INTERACTION WITH FLAGELLIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=3610;
RX PubMed=21895793; DOI=10.1111/j.1365-2958.2011.07822.x;
RA Mukherjee S., Yakhnin H., Kysela D., Sokoloski J., Babitzke P.,
RA Kearns D.B.;
RT "CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on
RT flagellar morphogenesis in Bacillus subtilis.";
RL Mol. Microbiol. 82:447-461(2011).
RN [6]
RP SUBUNIT, INTERACTION WITH FLAGELLIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=3610;
RX PubMed=23144244; DOI=10.1128/jb.01654-12;
RA Mukherjee S., Babitzke P., Kearns D.B.;
RT "FliW and FliS function independently to control cytoplasmic flagellin
RT levels in Bacillus subtilis.";
RL J. Bacteriol. 195:297-306(2013).
RN [7]
RP FUNCTION, AND INTERACTION WITH CSRA.
RC STRAIN=3610;
RX PubMed=27516547; DOI=10.1073/pnas.1602455113;
RA Mukherjee S., Oshiro R.T., Yakhnin H., Babitzke P., Kearns D.B.;
RT "FliW antagonizes CsrA RNA binding by a noncompetitive allosteric
RT mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9870-9875(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 (hag), which is implicated in polymerization, and
CC participates in the assembly of the flagellum (PubMed:16936039). An
CC antagonist to translational regulator CsrA, it binds CsrA at an
CC allosteric site and non-competitively inhibits CsrA binding to hag RNA
CC (PubMed:27516547). Partner switching by flagellin between FliW and CsrA
CC provides a flagellar assembly checkpoint to tightly control the timing
CC of flagellin synthesis. Flagellin binds to assembly factor FliW,
CC freeing translation regulator CsrA to repress translation of the
CC flagellin mRNA. When the flagellar hook is assembled flagellin is
CC secreted, depleting intracellular flagellin, which frees FliW to
CC interact with CsrA and inhibits CsrA binding to mRNA. This derepresses
CC flagellin translation and provides protein for flagellar assembly. Once
CC the flagellar filament is completed cytoplasmic flagellin levels rise
CC and CsrA translation repression of flagellin reinitiates
CC (PubMed:21895793). Binds to CsrA and displaces it from hag mRNA
CC (PubMed:21895793, PubMed:27516547). Binds to hag mRNA itself, but only
CC at much higher concentrations than those required to displace CsrA
CC (PubMed:21895793, PubMed:27516547). {ECO:0000269|PubMed:16936039,
CC ECO:0000269|PubMed:21895793, ECO:0000269|PubMed:27516547}.
CC -!- SUBUNIT: Interacts with flagellin in a 1:1 complex (PubMed:16936039,
CC PubMed:21895793). Two molecules interact with each CsrA dimer; cannot
CC interact with both flagellin and CsrA simultaneously (PubMed:21895793,
CC PubMed:27516547). Has a higher affinity for CsrA than for flagellin
CC (PubMed:21895793). Interacts directly with flagellin (hag), forms a 3-
CC way complex of Hag, FliS and FliW in which Flis and FliW do not
CC directly interact (PubMed:23144244). Interaction with Hag may occur via
CC the C-terminus of Hag (PubMed:16936039). {ECO:0000269|PubMed:16936039,
CC ECO:0000269|PubMed:21895793, ECO:0000269|PubMed:23144244,
CC ECO:0000269|PubMed:27516547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185,
CC ECO:0000305}.
CC -!- INDUCTION: Part of the SigD-controlled yvyF-csrA operon and the SigA-
CC controlled fliW-csrA operon (PubMed:17555441).
CC {ECO:0000269|PubMed:17555441}.
CC -!- DISRUPTION PHENOTYPE: Greatly reduced swarming motility, less flagellin
CC (PubMed:16936039, PubMed:21895793). Fewer, shorter flagella assemble
CC (PubMed:21895793). Loss of motility and flagellar assembly are
CC suppressed by deletion of csrA (PubMed:21895793). Decreased expression
CC of flagellin (Hag) which is suppressed by deletion of csrA
CC (PubMed:23144244). {ECO:0000269|PubMed:16936039,
CC ECO:0000269|PubMed:21895793, ECO:0000269|PubMed:23144244}.
CC -!- SIMILARITY: Belongs to the FliW family. {ECO:0000255|HAMAP-
CC Rule:MF_01185, ECO:0000305}.
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DR EMBL; U56901; AAC44949.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15555.1; -; Genomic_DNA.
DR PIR; C70042; C70042.
DR RefSeq; NP_391418.1; NC_000964.3.
DR RefSeq; WP_003228007.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P96503; -.
DR SMR; P96503; -.
DR STRING; 224308.BSU35380; -.
DR PaxDb; P96503; -.
DR PRIDE; P96503; -.
DR EnsemblBacteria; CAB15555; CAB15555; BSU_35380.
DR GeneID; 936732; -.
DR KEGG; bsu:BSU35380; -.
DR PATRIC; fig|224308.179.peg.3829; -.
DR eggNOG; COG1699; Bacteria.
DR InParanoid; P96503; -.
DR OMA; DVAVFCI; -.
DR PhylomeDB; P96503; -.
DR BioCyc; BSUB:BSU35380-MON; -.
DR Proteomes; UP000001570; 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:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:CACAO.
DR GO; GO:1902210; P:positive regulation of bacterial-type flagellum assembly; IMP:CACAO.
DR GO; GO:0045727; P:positive regulation of translation; IMP:CACAO.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IMP:CACAO.
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..143
FT /note="Flagellar assembly factor FliW"
FT /id="PRO_0000272970"
SQ SEQUENCE 143 AA; 16170 MW; 9AD134BCD3D156EF CRC64;
MIIHTKYHGQ MNIKEEQIIL FESGIPGFLE EKQFVILPLS EDSPFVALQS VTSENLAFIV
VSPFIFFKNY EFDLDESTAE LLDIDNIQDV EVMTILTMAE PFEKSTANLL APIIVNRKNM
MAKQVVLHDS SYTTKHPIGG ESC
