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P06179

- FLIC_SALTY

UniProt

P06179 - FLIC_SALTY

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Protein

Flagellin

Gene

fliC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. bacterial-type flagellum-dependent cell motility Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1970-MONOMER.
ReactomeiREACT_24954. NFkB and MAPK activation mediated by TRAF6.
REACT_27259. MyD88 cascade initiated on plasma membrane.
REACT_27287. TLR5 cascade.
REACT_75892. The IPAF inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Flagellin
Alternative name(s):
Phase 1-I flagellin
Gene namesi
Name:fliC
Synonyms:flaF, hag
Ordered Locus Names:STM1959
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. bacterial-type flagellum filament Source: InterPro
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Bacterial flagellum, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 495494FlagellinPRO_0000182578Add
BLAST

Proteomic databases

PaxDbiP06179.
PRIDEiP06179.

Expressioni

Inductioni

Inhibited in nutrient-poor medium (at protein level).1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
fliSP266096EBI-2011501,EBI-2011519

Protein-protein interaction databases

DIPiDIP-43768N.
IntActiP06179. 1 interaction.
MINTiMINT-2831235.
STRINGi99287.STM1959.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 9941
Helixi106 – 12924
Turni137 – 1393
Beta strandi142 – 1476
Beta strandi149 – 1513
Beta strandi155 – 1606
Turni165 – 1695
Beta strandi180 – 1856
Beta strandi190 – 1978
Helixi200 – 2023
Turni204 – 2063
Helixi208 – 2103
Beta strandi212 – 2176
Beta strandi219 – 2235
Turni225 – 2273
Beta strandi230 – 2378
Beta strandi244 – 2507
Turni252 – 2543
Beta strandi256 – 2605
Beta strandi277 – 2859
Helixi286 – 2883
Helixi290 – 2989
Beta strandi305 – 3139
Beta strandi319 – 32810
Beta strandi331 – 3377
Beta strandi343 – 3453
Beta strandi353 – 3564
Beta strandi361 – 3666
Beta strandi371 – 3766
Beta strandi379 – 3824
Helixi383 – 3864
Turni391 – 3933
Helixi408 – 44841

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IO1X-ray2.00A54-451[»]
1P95model-A57-451[»]
1UCUelectron microscopy4.00A2-495[»]
3A5Xelectron microscopy4.00A2-495[»]
DisProtiDP00026.
ProteinModelPortaliP06179.
SMRiP06179. Positions 2-495.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06179.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial flagellin family.Curated

Phylogenomic databases

eggNOGiCOG1344.
HOGENOMiHOG000255144.
KOiK02406.
OMAiCGANANV.
OrthoDBiEOG6M9DVB.
PhylomeDBiP06179.

Family and domain databases

InterProiIPR001492. Flagellin.
IPR001029. Flagellin_D0/D1.
IPR014981. Flagellin_D3.
[Graphical view]
PfamiPF00700. Flagellin_C. 1 hit.
PF08884. Flagellin_D3. 1 hit.
PF00669. Flagellin_N. 1 hit.
[Graphical view]
PRINTSiPR00207. FLAGELLIN.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06179-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI
60 70 80 90 100
ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNLQ RVRELAVQSA
110 120 130 140 150
NSTNSQSDLD SIQAEITQRL NEIDRVSGQT QFNGVKVLAQ DNTLTIQVGA
160 170 180 190 200
NDGETIDIDL KQINSQTLGL DTLNVQQKYK VSDTAATVTG YADTTIALDN
210 220 230 240 250
STFKASATGL GGTDQKIDGD LKFDDTTGKY YAKVTVTGGT GKDGYYEVSV
260 270 280 290 300
DKTNGEVTLA GGATSPLTGG LPATATEDVK NVQVANADLT EAKAALTAAG
310 320 330 340 350
VTGTASVVKM SYTDNNGKTI DGGLAVKVGD DYYSATQNKD GSISINTTKY
360 370 380 390 400
TADDGTSKTA LNKLGGADGK TEVVSIGGKT YAASKAEGHN FKAQPDLAEA
410 420 430 440 450
AATTTENPLQ KIDAALAQVD TLRSDLGAVQ NRFNSAITNL GNTVNNLTSA
460 470 480 490
RSRIEDSDYA TEVSNMSRAQ ILQQAGTSVL AQANQVPQNV LSLLR
Length:495
Mass (Da):51,612
Last modified:January 23, 2007 - v4
Checksum:i4BD7849FA3B936BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271S → N in AAA27072. (PubMed:2999134)Curated
Sequence conflicti133 – 1331N → S in AAA27072. (PubMed:2999134)Curated
Sequence conflicti215 – 2151Q → E in AAA27072. (PubMed:2999134)Curated
Sequence conflicti261 – 27313GGATS…GGLPA → AVTPATVT in AAA27072. (PubMed:2999134)CuratedAdd
BLAST
Sequence conflicti277 – 2848EDVKNVQV → ALSGKMYS in AAA27072. (PubMed:2999134)Curated
Sequence conflicti287 – 2915ADLTE → PDSDI in AAA27072. (PubMed:2999134)Curated
Sequence conflicti338 – 3381N → D in AAA27072. (PubMed:2999134)Curated
Sequence conflicti346 – 3461N → D in AAA27072. (PubMed:2999134)Curated
Sequence conflicti354 – 3541D → N in AAA27072. (PubMed:2999134)Curated
Sequence conflicti375 – 3773SIG → TID in AAA27072. (PubMed:2999134)Curated
Sequence conflicti382 – 3821A → N in AAA27072. (PubMed:2999134)Curated
Sequence conflicti387 – 3871E → A in AAA27072. (PubMed:2999134)Curated
Sequence conflicti390 – 3901N → D in AAA27072. (PubMed:2999134)Curated
Sequence conflicti394 – 3963QPD → EPE in AAA27072. (PubMed:2999134)Curated
Sequence conflicti400 – 4001A → Q in AAA27072. (PubMed:2999134)Curated
Sequence conflicti403 – 4031T → K in AAA27072. (PubMed:2999134)Curated
Sequence conflicti448 – 4481T → S in AAA27072. (PubMed:2999134)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11332 Genomic DNA. Translation: AAA27072.1.
D13689 Genomic DNA. Translation: BAA02846.1.
AE006468 Genomic DNA. Translation: AAL20871.1.
X51740 Genomic DNA. Translation: CAA36029.1.
J01801 Genomic DNA. Translation: AAA27074.1.
M33808 Genomic DNA. Translation: AAA27080.1.
Z54217 Genomic DNA. Translation: CAA90950.1.
PIRiA24262.
S16121.
RefSeqiNP_460912.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20871; AAL20871; STM1959.
GeneIDi1253480.
KEGGistm:STM1959.
PATRICi32382477. VBISalEnt20916_2074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11332 Genomic DNA. Translation: AAA27072.1 .
D13689 Genomic DNA. Translation: BAA02846.1 .
AE006468 Genomic DNA. Translation: AAL20871.1 .
X51740 Genomic DNA. Translation: CAA36029.1 .
J01801 Genomic DNA. Translation: AAA27074.1 .
M33808 Genomic DNA. Translation: AAA27080.1 .
Z54217 Genomic DNA. Translation: CAA90950.1 .
PIRi A24262.
S16121.
RefSeqi NP_460912.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IO1 X-ray 2.00 A 54-451 [» ]
1P95 model - A 57-451 [» ]
1UCU electron microscopy 4.00 A 2-495 [» ]
3A5X electron microscopy 4.00 A 2-495 [» ]
DisProti DP00026.
ProteinModelPortali P06179.
SMRi P06179. Positions 2-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-43768N.
IntActi P06179. 1 interaction.
MINTi MINT-2831235.
STRINGi 99287.STM1959.

Proteomic databases

PaxDbi P06179.
PRIDEi P06179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20871 ; AAL20871 ; STM1959 .
GeneIDi 1253480.
KEGGi stm:STM1959.
PATRICi 32382477. VBISalEnt20916_2074.

Phylogenomic databases

eggNOGi COG1344.
HOGENOMi HOG000255144.
KOi K02406.
OMAi CGANANV.
OrthoDBi EOG6M9DVB.
PhylomeDBi P06179.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-1970-MONOMER.
Reactomei REACT_24954. NFkB and MAPK activation mediated by TRAF6.
REACT_27259. MyD88 cascade initiated on plasma membrane.
REACT_27287. TLR5 cascade.
REACT_75892. The IPAF inflammasome.

Miscellaneous databases

EvolutionaryTracei P06179.

Family and domain databases

InterProi IPR001492. Flagellin.
IPR001029. Flagellin_D0/D1.
IPR014981. Flagellin_D3.
[Graphical view ]
Pfami PF00700. Flagellin_C. 1 hit.
PF08884. Flagellin_D3. 1 hit.
PF00669. Flagellin_N. 1 hit.
[Graphical view ]
PRINTSi PR00207. FLAGELLIN.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The covalent structure of the phase-1 flagellar filament protein of Salmonella typhimurium and its comparison with other flagellins."
    Joys T.M.
    J. Biol. Chem. 260:15758-15761(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Amino acids responsible for flagellar shape are distributed in terminal regions of flagellin."
    Kanto S., Okino H., Aizawa S., Yamaguchi S.
    J. Mol. Biol. 219:471-480(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Conversion of the Salmonella phase 1 flagellin gene fliC to the phase 2 gene fljB on the Escherichia coli K-12 chromosome."
    Okazaki N., Matsuo S., Saito K., Tominaga A., Enomoto M.
    J. Bacteriol. 175:758-766(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  5. "Flagellar hook and hook-associated proteins of Salmonella typhimurium and their relationship to other axial components of the flagellum."
    Homma M., Derosier D.J., Macnab R.M.
    J. Mol. Biol. 213:819-832(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  6. "Analysis of the nucleotide sequence of an invertible controlling element."
    Zieg J., Simon M.
    Proc. Natl. Acad. Sci. U.S.A. 77:4196-4200(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
  7. "Sequence invariance of the antigen-coding central region of the phase 1 flagellar filament gene (fliC) among strains of Salmonella typhimurium."
    Smith N.H., Selander R.K.
    J. Bacteriol. 172:603-609(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-428.
  8. "Point mutations that lock Salmonella typhimurium flagellar filaments in the straight right-handed and left-handed forms and their relation to filament superhelicity."
    Hyman H.C., Trachtenberg S.
    J. Mol. Biol. 220:79-88(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 411-495.
  9. "The flagellin N-methylase gene fliB and an adjacent serovar-specific IS200 element in Salmonella typhimurium."
    Burnens A.P., Stanley J., Sack R., Hunziker P., Brodard I., Nicolet J.
    Microbiology 143:1539-1547(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-495.
    Strain: LT2 / ATCC 23564.
  10. "EAL domain protein YdiV acts as an anti-FlhD4C2 factor responsible for nutritional control of the flagellar regulon in Salmonella enterica Serovar Typhimurium."
    Wada T., Morizane T., Abo T., Tominaga A., Inoue-Tanaka K., Kutsukake K.
    J. Bacteriol. 193:1600-1611(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiFLIC_SALTY
AccessioniPrimary (citable) accession number: P06179
Secondary accession number(s): P97160, Q02871, Q56088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Individual Salmonella serotypes usually alternate between the production of 2 antigenic forms of flagella, termed phase 1 and phase 2, each specified by separate structural genes, fliC and fljB.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3