FLA_BACSU
ID FLA_BACSU Reviewed; 304 AA.
AC P02968;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Flagellin;
DE AltName: Full=GSX1 {ECO:0000303|PubMed:7768864};
DE AltName: Full=Hag;
GN Name=hag {ECO:0000303|PubMed:2498283}; OrderedLocusNames=BSU35360;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=168;
RX PubMed=814121; DOI=10.1016/s0021-9258(17)33840-1;
RA Delange R.J., Chang J.Y., Shaper J.H., Glazer A.N.;
RT "Amino acid sequence of flagellin of Bacillus subtilis 168. III. Tryptic
RT peptides, N-bromosuccinimide peptides, and the complete amino acid
RT sequence.";
RL J. Biol. Chem. 251:705-711(1976).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2498283; DOI=10.1128/jb.171.6.3085-3094.1989;
RA Lavallie E.R., Stahl M.L.;
RT "Cloning of the flagellin gene from Bacillus subtilis and complementation
RT studies of an in vitro-derived deletion mutation.";
RL J. Bacteriol. 171:3085-3094(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2498284; DOI=10.1128/jb.171.6.3095-3101.1989;
RA Mirel D.B., Chamberlin M.J.;
RT "The Bacillus subtilis flagellin gene (hag) is transcribed by the sigma 28
RT form of RNA polymerase.";
RL J. Bacteriol. 171:3095-3101(1989).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-15.
RX PubMed=7768864; DOI=10.1128/jb.177.12.3540-3545.1995;
RA Antelmann H., Bernhardt J., Schmid R., Hecker M.;
RT "A gene at 333 degrees on the Bacillus subtilis chromosome encodes the
RT newly identified sigma B-dependent general stress protein GspA.";
RL J. Bacteriol. 177:3540-3545(1995).
RN [7]
RP PROTEIN SEQUENCE OF 1-19.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=8180695; DOI=10.1099/13500872-140-2-297;
RA Hartford O.M., Dowds B.C.A.;
RT "Isolation and characterization of a hydrogen peroxide resistant mutant of
RT Bacillus subtilis.";
RL Microbiology 140:297-304(1994).
RN [8]
RP PROTEIN SEQUENCE OF 1-11, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
RN [9]
RP PROTEIN SEQUENCE OF 1-10, AND 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 [10]
RP INDUCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=11987133;
RX DOI=10.1002/1615-9861(200205)2:5<591::aid-prot591>3.0.co;2-8;
RA Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.;
RT "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic
RT approach.";
RL Proteomics 2:591-602(2002).
RN [11]
RP FLAGELLAR ASSEMBLY, INTERACTION WITH FLIW, AND MUTAGENESIS OF ASN-255.
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 [12]
RP FUNCTION IN AUTOREGULATION, AND INTERACTION WITH FLIW.
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 [13]
RP SUBUNIT, INTERACTION WITH FLIS, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Flagellin is the subunit which polymerizes to form the
CC filaments of bacterial flagella. Assembly into flagella requires FliW
CC (PubMed:16936039). Acts as a homeostatic autoinhibitory regulator to
CC control its own cytoplasmic levels. Partner switching by flagellin
CC between FliW and CsrA provides a flagellar assembly checkpoint to
CC tightly control the timing of flagellin synthesis. Flagellin binds to
CC assembly factor FliW, freeing translation regulator CsrA to repress
CC translation of the flagellin mRNA. When the flagellar hook is assembled
CC flagellin is secreted, depleting intracellular flagellin, which frees
CC FliW to interact with CsrA. This derepresses flagellin translation and
CC provides protein for flagellar assembly. Once the flagellar filament is
CC completed cytoplasmic flagellin levels rise and CsrA translation
CC repression of flagellin reinitiates (PubMed:21895793).
CC {ECO:0000269|PubMed:16936039, ECO:0000269|PubMed:21895793}.
CC -!- SUBUNIT: Interacts with FliW in a 1:1 complex (PubMed:16936039,
CC PubMed:21895793). Forms a 3-way complex of Hag, FliS and FliW, in which
CC Flis and FliW do not directly interact (PubMed:23144244).
CC {ECO:0000269|PubMed:21895793, ECO:0000269|PubMed:23144244,
CC ECO:0000269|PubMed:7768864}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23144244}. Bacterial
CC flagellum. Secreted, cell wall {ECO:0000269|PubMed:11987133}. Note=Cell
CC wall localization shown in PubMed:11987133.
CC -!- INDUCTION: Under positive control of SigD (PubMed:11987133). Repressed
CC by CsrA; repression is greater in the 1A96 than 168 genetic background
CC and higher in minimal than rich medium (PubMed:17555441).
CC {ECO:0000269|PubMed:11987133, ECO:0000269|PubMed:17555441}.
CC -!- SIMILARITY: Belongs to the bacterial flagellin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26947; AAA22437.1; -; Genomic_DNA.
DR EMBL; M26948; AAA22509.1; -; Genomic_DNA.
DR EMBL; U56901; AAC44951.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15553.1; -; Genomic_DNA.
DR PIR; A44759; FLBS68.
DR RefSeq; NP_391416.1; NC_000964.3.
DR RefSeq; WP_003228021.1; NZ_JNCM01000033.1.
DR PDB; 5MAW; X-ray; 1.50 A; D=2-304.
DR PDB; 5WJT; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-304.
DR PDB; 6GOW; X-ray; 2.10 A; D=1-304.
DR PDBsum; 5MAW; -.
DR PDBsum; 5WJT; -.
DR PDBsum; 6GOW; -.
DR AlphaFoldDB; P02968; -.
DR SMR; P02968; -.
DR DIP; DIP-59540N; -.
DR IntAct; P02968; 2.
DR MINT; P02968; -.
DR STRING; 224308.BSU35360; -.
DR jPOST; P02968; -.
DR PaxDb; P02968; -.
DR PRIDE; P02968; -.
DR EnsemblBacteria; CAB15553; CAB15553; BSU_35360.
DR GeneID; 936742; -.
DR KEGG; bsu:BSU35360; -.
DR PATRIC; fig|224308.179.peg.3827; -.
DR eggNOG; COG1344; Bacteria.
DR InParanoid; P02968; -.
DR OMA; MAERNAM; -.
DR PhylomeDB; P02968; -.
DR BioCyc; BSUB:BSU35360-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR001492; Flagellin.
DR InterPro; IPR046358; Flagellin_C.
DR InterPro; IPR001029; Flagellin_N.
DR PANTHER; PTHR42792; PTHR42792; 1.
DR Pfam; PF00700; Flagellin_C; 1.
DR Pfam; PF00669; Flagellin_N; 1.
DR PRINTS; PR00207; FLAGELLIN.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Cell wall; Direct protein sequencing;
KW Reference proteome; Secreted.
FT CHAIN 1..304
FT /note="Flagellin"
FT /id="PRO_0000182585"
FT MUTAGEN 255
FT /note="N->A: Peptide of residues 247-265 no longer binds
FT FliW."
FT /evidence="ECO:0000269|PubMed:16936039"
FT CONFLICT 101..102
FT /note="GT -> TG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 46..97
FT /evidence="ECO:0007829|PDB:5MAW"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5MAW"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 108..129
FT /evidence="ECO:0007829|PDB:5MAW"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5MAW"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5MAW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5MAW"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:5MAW"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:5MAW"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6GOW"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:5MAW"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 214..257
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 266..282
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:5MAW"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:5MAW"
SQ SEQUENCE 304 AA; 32626 MW; A28AEFFDB1316684 CRC64;
MRINHNIAAL NTLNRLSSNN SASQKNMEKL SSGLRINRAG DDAAGLAISE KMRGQIRGLE
MASKNSQDGI SLIQTAEGAL TETHAILQRV RELVVQAGNT GTQDKATDLQ SIQDEISALT
DEIDGISNRT EFNGKKLLDG TYKVDTATPA NQKNLVFQIG ANATQQISVN IEDMGADALG
IKEADGSIAA LHSVNDLDVT KFADNAADTA DIGFDAQLKV VDEAINQVSS QRAKLGAVQN
RLEHTINNLS ASGENLTAAE SRIRDVDMAK EMSEFTKNNI LSQASQAMLA QANQQPQNVL
QLLR
