FLIC_SALTY
ID FLIC_SALTY Reviewed; 495 AA.
AC P06179; P97160; Q02871; Q56088;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Flagellin;
DE AltName: Full=Phase 1-I flagellin;
GN Name=fliC; Synonyms=flaF, hag; OrderedLocusNames=STM1959;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999134; DOI=10.1016/s0021-9258(17)36323-8;
RA Joys T.M.;
RT "The covalent structure of the phase-1 flagellar filament protein of
RT Salmonella typhimurium and its comparison with other flagellins.";
RL J. Biol. Chem. 260:15758-15761(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2051483; DOI=10.1016/0022-2836(91)90187-b;
RA Kanto S., Okino H., Aizawa S., Yamaguchi S.;
RT "Amino acids responsible for flagellar shape are distributed in terminal
RT regions of flagellin.";
RL J. Mol. Biol. 219:471-480(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8423149; DOI=10.1128/jb.175.3.758-766.1993;
RA Okazaki N., Matsuo S., Saito K., Tominaga A., Enomoto M.;
RT "Conversion of the Salmonella phase 1 flagellin gene fliC to the phase 2
RT gene fljB on the Escherichia coli K-12 chromosome.";
RL J. Bacteriol. 175:758-766(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2193164; DOI=10.1016/s0022-2836(05)80266-9;
RA Homma M., Derosier D.J., Macnab R.M.;
RT "Flagellar hook and hook-associated proteins of Salmonella typhimurium and
RT their relationship to other axial components of the flagellum.";
RL J. Mol. Biol. 213:819-832(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=6933466; DOI=10.1073/pnas.77.7.4196;
RA Zieg J., Simon M.;
RT "Analysis of the nucleotide sequence of an invertible controlling
RT element.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:4196-4200(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-428.
RX PubMed=2404944; DOI=10.1128/jb.172.2.603-609.1990;
RA Smith N.H., Selander R.K.;
RT "Sequence invariance of the antigen-coding central region of the phase 1
RT flagellar filament gene (fliC) among strains of Salmonella typhimurium.";
RL J. Bacteriol. 172:603-609(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 411-495.
RX PubMed=2067020; DOI=10.1016/0022-2836(91)90382-g;
RA Hyman H.C., Trachtenberg S.;
RT "Point mutations that lock Salmonella typhimurium flagellar filaments in
RT the straight right-handed and left-handed forms and their relation to
RT filament superhelicity.";
RL J. Mol. Biol. 220:79-88(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-495.
RC STRAIN=LT2 / ATCC 23564;
RX PubMed=9168604; DOI=10.1099/00221287-143-5-1539;
RA Burnens A.P., Stanley J., Sack R., Hunziker P., Brodard I., Nicolet J.;
RT "The flagellin N-methylase gene fliB and an adjacent serovar-specific IS200
RT element in Salmonella typhimurium.";
RL Microbiology 143:1539-1547(1997).
RN [10]
RP INDUCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=21278297; DOI=10.1128/jb.01494-10;
RA Wada T., Morizane T., Abo T., Tominaga A., Inoue-Tanaka K., Kutsukake K.;
RT "EAL domain protein YdiV acts as an anti-FlhD4C2 factor responsible for
RT nutritional control of the flagellar regulon in Salmonella enterica Serovar
RT Typhimurium.";
RL J. Bacteriol. 193:1600-1611(2011).
CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to form
CC the filaments of bacterial flagella.
CC -!- INTERACTION:
CC P06179; P26609: fliS; NbExp=6; IntAct=EBI-2011501, EBI-2011519;
CC P06179; P0A1N2: fliT; NbExp=2; IntAct=EBI-2011501, EBI-15610664;
CC P06179; Q9R016: Naip5; Xeno; NbExp=9; IntAct=EBI-2011501, EBI-15944130;
CC -!- SUBCELLULAR LOCATION: Secreted. Bacterial flagellum.
CC -!- INDUCTION: Inhibited in nutrient-poor medium (at protein level).
CC {ECO:0000269|PubMed:21278297}.
CC -!- MISCELLANEOUS: Individual Salmonella serotypes usually alternate
CC between the production of 2 antigenic forms of flagella, termed phase 1
CC and phase 2, each specified by separate structural genes, fliC and
CC fljB.
CC -!- SIMILARITY: Belongs to the bacterial flagellin family. {ECO:0000305}.
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DR EMBL; M11332; AAA27072.1; -; Genomic_DNA.
DR EMBL; D13689; BAA02846.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20871.1; -; Genomic_DNA.
DR EMBL; X51740; CAA36029.1; -; Genomic_DNA.
DR EMBL; J01801; AAA27074.1; -; Genomic_DNA.
DR EMBL; M33808; AAA27080.1; -; Genomic_DNA.
DR EMBL; Z54217; CAA90950.1; -; Genomic_DNA.
DR PIR; A24262; A24262.
DR PIR; S16121; S16121.
DR RefSeq; NP_460912.1; NC_003197.2.
DR RefSeq; WP_000079805.1; NC_003197.2.
DR PDB; 1IO1; X-ray; 2.00 A; A=54-451.
DR PDB; 1UCU; EM; 4.00 A; A=2-495.
DR PDB; 3A5X; EM; 4.00 A; A=2-495.
DR PDB; 5YUD; EM; 4.28 A; C=452-495.
DR PDB; 6CH3; X-ray; 2.68 A; B=431-495.
DR PDBsum; 1IO1; -.
DR PDBsum; 1UCU; -.
DR PDBsum; 3A5X; -.
DR PDBsum; 5YUD; -.
DR PDBsum; 6CH3; -.
DR AlphaFoldDB; P06179; -.
DR SMR; P06179; -.
DR DIP; DIP-43768N; -.
DR IntAct; P06179; 6.
DR MINT; P06179; -.
DR STRING; 99287.STM1959; -.
DR PaxDb; P06179; -.
DR EnsemblBacteria; AAL20871; AAL20871; STM1959.
DR GeneID; 1253480; -.
DR KEGG; stm:STM1959; -.
DR PATRIC; fig|99287.12.peg.2074; -.
DR HOGENOM; CLU_011142_7_2_6; -.
DR OMA; MAERNAM; -.
DR PhylomeDB; P06179; -.
DR BioCyc; SENT99287:STM1959-MON; -.
DR Reactome; R-GGA-433822; NFkB and MAPK activation mediated by TRAF6.
DR Reactome; R-GGA-451534; TLR5 cascade.
DR Reactome; R-GGA-977240; MyD88 cascade initiated on plasma membrane.
DR Reactome; R-HSA-844623; The IPAF inflammasome.
DR EvolutionaryTrace; P06179; -.
DR PHI-base; PHI:6462; -.
DR PHI-base; PHI:7449; -.
DR PHI-base; PHI:7576; -.
DR PHI-base; PHI:8372; -.
DR Proteomes; UP000001014; 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 DisProt; DP00026; -.
DR Gene3D; 6.10.10.10; -; 1.
DR InterPro; IPR001492; Flagellin.
DR InterPro; IPR046358; Flagellin_C.
DR InterPro; IPR042187; Flagellin_C_sub2.
DR InterPro; IPR014981; Flagellin_D3.
DR InterPro; IPR001029; Flagellin_N.
DR PANTHER; PTHR42792; PTHR42792; 1.
DR Pfam; PF00700; Flagellin_C; 1.
DR Pfam; PF08884; Flagellin_D3; 1.
DR Pfam; PF00669; Flagellin_N; 1.
DR PRINTS; PR00207; FLAGELLIN.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..495
FT /note="Flagellin"
FT /id="PRO_0000182578"
FT CONFLICT 127
FT /note="S -> N (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="N -> S (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="Q -> E (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..273
FT /note="GGATSPLTGGLPA -> AVTPATVT (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..284
FT /note="EDVKNVQV -> ALSGKMYS (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..291
FT /note="ADLTE -> PDSDI (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="N -> D (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="N -> D (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="D -> N (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 375..377
FT /note="SIG -> TID (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> N (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="E -> A (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="N -> D (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..396
FT /note="QPD -> EPE (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="A -> Q (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="T -> K (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="T -> S (in Ref. 1; AAA27072)"
FT /evidence="ECO:0000305"
FT HELIX 59..99
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 106..129
FT /evidence="ECO:0007829|PDB:1IO1"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1IO1"
FT TURN 165..169
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1IO1"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1IO1"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:1IO1"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:1IO1"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1IO1"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 408..448
FT /evidence="ECO:0007829|PDB:1IO1"
FT HELIX 458..473
FT /evidence="ECO:0007829|PDB:6CH3"
FT HELIX 475..482
FT /evidence="ECO:0007829|PDB:6CH3"
FT HELIX 487..494
FT /evidence="ECO:0007829|PDB:6CH3"
SQ SEQUENCE 495 AA; 51612 MW; 4BD7849FA3B936BA CRC64;
MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG
LTQASRNAND GISIAQTTEG ALNEINNNLQ RVRELAVQSA NSTNSQSDLD SIQAEITQRL
NEIDRVSGQT QFNGVKVLAQ DNTLTIQVGA NDGETIDIDL KQINSQTLGL DTLNVQQKYK
VSDTAATVTG YADTTIALDN STFKASATGL GGTDQKIDGD LKFDDTTGKY YAKVTVTGGT
GKDGYYEVSV DKTNGEVTLA GGATSPLTGG LPATATEDVK NVQVANADLT EAKAALTAAG
VTGTASVVKM SYTDNNGKTI DGGLAVKVGD DYYSATQNKD GSISINTTKY TADDGTSKTA
LNKLGGADGK TEVVSIGGKT YAASKAEGHN FKAQPDLAEA AATTTENPLQ KIDAALAQVD
TLRSDLGAVQ NRFNSAITNL GNTVNNLTSA RSRIEDSDYA TEVSNMSRAQ ILQQAGTSVL
AQANQVPQNV LSLLR
