FLIS_BACSU
ID FLIS_BACSU Reviewed; 133 AA.
AC P39739;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Flagellar secretion chaperone FliS;
GN Name=fliS; OrderedLocusNames=BSU35330;
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 / HB2058;
RX PubMed=8195064; DOI=10.1128/jb.176.11.3093-3101.1994;
RA Chen L., Helmann J.D.;
RT "The Bacillus subtilis sigma D-dependent operon encoding the flagellar
RT proteins FliD, FliS, and FliT.";
RL J. Bacteriol. 176:3093-3101(1994).
RN [2]
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 [3]
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 [4]
RP FUNCTION, 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 [5] {ECO:0007744|PDB:1VH6}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-133, AND SUBUNIT.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Essential for filament assembly (PubMed:23144244). May act as
CC a facilitator of flagellin (hag) secretion. Antagonizes translational
CC repressor CsrA indirectly (PubMed:23144244).
CC {ECO:0000269|PubMed:23144244}.
CC -!- SUBUNIT: Homodimer (PubMed:23144244, PubMed:16021622). Interacts
CC directly with flagellin (hag), forms a 3-way complex of Hag, FliS and
CC FliW in which Flis and FliW do not directly interact (PubMed:23144244).
CC {ECO:0000269|PubMed:23144244, ECO:0000305|PubMed:16021622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Severe defect in motility on agar plates, forms
CC multiple short filament stubs on the cell surface, decreased expression
CC of flagellin (hag), 30-fold decrease in Hag secretion. All phenotypes
CC are partially suppressed by deletion of csrA, which increases
CC translation of Hag (PubMed:23144244). {ECO:0000269|PubMed:23144244}.
CC -!- SIMILARITY: Belongs to the FliS family. {ECO:0000305}.
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DR EMBL; Z31376; CAA83249.1; -; Genomic_DNA.
DR EMBL; U56901; AAC44954.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15550.1; -; Genomic_DNA.
DR PIR; I40398; I40398.
DR RefSeq; NP_391413.1; NC_000964.3.
DR RefSeq; WP_003243747.1; NZ_JNCM01000033.1.
DR PDB; 1VH6; X-ray; 2.50 A; A/B=2-133.
DR PDB; 5MAW; X-ray; 1.50 A; E=1-133.
DR PDB; 6GOW; X-ray; 2.10 A; E=1-133.
DR PDBsum; 1VH6; -.
DR PDBsum; 5MAW; -.
DR PDBsum; 6GOW; -.
DR AlphaFoldDB; P39739; -.
DR SMR; P39739; -.
DR DIP; DIP-59541N; -.
DR IntAct; P39739; 1.
DR STRING; 224308.BSU35330; -.
DR PaxDb; P39739; -.
DR PRIDE; P39739; -.
DR EnsemblBacteria; CAB15550; CAB15550; BSU_35330.
DR GeneID; 936720; -.
DR KEGG; bsu:BSU35330; -.
DR PATRIC; fig|224308.179.peg.3824; -.
DR eggNOG; COG1516; Bacteria.
DR InParanoid; P39739; -.
DR OMA; EFRDTWK; -.
DR PhylomeDB; P39739; -.
DR BioCyc; BSUB:BSU35330-MON; -.
DR EvolutionaryTrace; P39739; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR CDD; cd16098; FliS; 1.
DR InterPro; IPR003713; FliS.
DR InterPro; IPR036584; FliS_sf.
DR PANTHER; PTHR34773; PTHR34773; 1.
DR Pfam; PF02561; FliS; 1.
DR PIRSF; PIRSF039090; Flis; 1.
DR SUPFAM; SSF101116; SSF101116; 1.
DR TIGRFAMs; TIGR00208; fliS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum biogenesis; Chaperone; Cytoplasm;
KW Reference proteome.
FT CHAIN 1..133
FT /note="Flagellar secretion chaperone FliS"
FT /id="PRO_0000180970"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 20..43
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 47..66
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:5MAW"
SQ SEQUENCE 133 AA; 15131 MW; E0E80476A96F14D3 CRC64;
MAIQNPYTAY QQNSVNTATP GELTLMLYNG CLKFIRLAAQ AIENDDMERK NENLIKAQNI
IQELNFTLNR NIELSASMGA MYDYMYRRLV QANIKNDTGM LAEVEGYVTD FRDAWKQAIQ
SERKDRHGSG GIA
