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P06179 (FLIC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flagellin
Alternative name(s):
Phase 1-I flagellin
Gene names
Name:fliC
Synonyms:flaF, hag
Ordered Locus Names:STM1959
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Secreted. Bacterial flagellum.

Induction

Inhibited in nutrient-poor medium (at protein level). Ref.10

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.

Sequence similarities

Belongs to the bacterial flagellin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fliSP266094EBI-2011501,EBI-2011519

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 495494Flagellin
PRO_0000182578

Experimental info

Sequence conflict1271S → N in AAA27072. Ref.1
Sequence conflict1331N → S in AAA27072. Ref.1
Sequence conflict2151Q → E in AAA27072. Ref.1
Sequence conflict261 – 27313GGATS…GGLPA → AVTPATVT in AAA27072. Ref.1
Sequence conflict277 – 2848EDVKNVQV → ALSGKMYS in AAA27072. Ref.1
Sequence conflict287 – 2915ADLTE → PDSDI in AAA27072. Ref.1
Sequence conflict3381N → D in AAA27072. Ref.1
Sequence conflict3461N → D in AAA27072. Ref.1
Sequence conflict3541D → N in AAA27072. Ref.1
Sequence conflict375 – 3773SIG → TID in AAA27072. Ref.1
Sequence conflict3821A → N in AAA27072. Ref.1
Sequence conflict3871E → A in AAA27072. Ref.1
Sequence conflict3901N → D in AAA27072. Ref.1
Sequence conflict394 – 3963QPD → EPE in AAA27072. Ref.1
Sequence conflict4001A → Q in AAA27072. Ref.1
Sequence conflict4031T → K in AAA27072. Ref.1
Sequence conflict4481T → S in AAA27072. Ref.1

Secondary structure

................................................................. 495
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06179 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 4BD7849FA3B936BA

FASTA49551,612
        10         20         30         40         50         60 
MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG 

        70         80         90        100        110        120 
LTQASRNAND GISIAQTTEG ALNEINNNLQ RVRELAVQSA NSTNSQSDLD SIQAEITQRL 

       130        140        150        160        170        180 
NEIDRVSGQT QFNGVKVLAQ DNTLTIQVGA NDGETIDIDL KQINSQTLGL DTLNVQQKYK 

       190        200        210        220        230        240 
VSDTAATVTG YADTTIALDN STFKASATGL GGTDQKIDGD LKFDDTTGKY YAKVTVTGGT 

       250        260        270        280        290        300 
GKDGYYEVSV DKTNGEVTLA GGATSPLTGG LPATATEDVK NVQVANADLT EAKAALTAAG 

       310        320        330        340        350        360 
VTGTASVVKM SYTDNNGKTI DGGLAVKVGD DYYSATQNKD GSISINTTKY TADDGTSKTA 

       370        380        390        400        410        420 
LNKLGGADGK TEVVSIGGKT YAASKAEGHN FKAQPDLAEA AATTTENPLQ KIDAALAQVD 

       430        440        450        460        470        480 
TLRSDLGAVQ NRFNSAITNL GNTVNNLTSA RSRIEDSDYA TEVSNMSRAQ ILQQAGTSVL 

       490 
AQANQVPQNV LSLLR 

« Hide

References

« Hide 'large scale' references
[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]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA24262.
S16121.
RefSeqNP_460912.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IO1X-ray2.00A54-450[»]
1P95model-A57-451[»]
1UCUelectron microscopy4.00A2-494[»]
3A5Xelectron microscopy4.00A2-495[»]
DisProtDP00026.
ProteinModelPortalP06179.
SMRP06179. Positions 2-495.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-43768N.
IntActP06179. 1 interaction.
MINTMINT-2831235.
STRING99287.STM1959.

Proteomic databases

PaxDbP06179.
PRIDEP06179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20871; AAL20871; STM1959.
GeneID1253480.
KEGGstm:STM1959.
PATRIC32382477. VBISalEnt20916_2074.

Phylogenomic databases

eggNOGCOG1344.
HOGENOMHOG000255144.
KOK02406.
OMAIASTEWS.
ProtClustDBPRK08026.

Enzyme and pathway databases

ReactomeREACT_147795. Innate Immune System.
REACT_6900. Immune System.
REACT_75813. Ipaf is activated.

Family and domain databases

InterProIPR001492. Flagellin.
IPR001029. Flagellin_D0/D1.
IPR014981. Flagellin_D3.
[Graphical view]
PfamPF00700. Flagellin_C. 1 hit.
PF08884. Flagellin_D3. 1 hit.
PF00669. Flagellin_N. 1 hit.
[Graphical view]
PRINTSPR00207. FLAGELLIN.
ProtoNetSearch...

Other

EvolutionaryTraceP06179.

Entry information

Entry nameFLIC_SALTY
AccessionPrimary (citable) accession number: P06179
Secondary accession number(s): P97160, Q02871, Q56088
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families