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P26465 (FLII_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 108. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flagellum-specific ATP synthase

EC=3.6.3.14
Gene names
Name:fliI
Synonyms:fla AIII, flaC
Ordered Locus Names:STM1972
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage.

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Flagellum-specific ATP synthase
PRO_0000144695

Regions

Nucleotide binding182 – 1898ATP By similarity

Experimental info

Mutagenesis1881K → E: Loss of flagellum.
Mutagenesis1881K → I: Loss of flagellum.
Mutagenesis2721D → N: Loss of flagellum.
Mutagenesis3631Y → S: Loss of flagellum.

Secondary structure

........................................................................ 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26465 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 830867B657592BF1

FASTA45649,265
        10         20         30         40         50         60 
MTTRLTRWLT ALDNFEAKMA LLPAVRRYGR LTRATGLVLE ATGLQLPLGA TCIIERQDGP 

        70         80         90        100        110        120 
ETKEVESEVV GFNGQRLFLM PLEEVEGILP GARVYARNGH GDGLQSGKQL PLGPALLGRV 

       130        140        150        160        170        180 
LDGGGKPLDG LPAPDTLETG ALITPPFNPL QRTPIEHVLD TGVRAINALL TVGRGQRMGL 

       190        200        210        220        230        240 
FAGSGVGKSV LLGMMARYTR ADVIVVGLIG ERGREVKDFI ENILGPDGRA RSVVIAAPAD 

       250        260        270        280        290        300 
VSPLLRMQGA AYATRIAEDF RDRGQHVLLI MDSLTRYAMA QREIALAIGE PPATKGYPPS 

       310        320        330        340        350        360 
VFAKLPALVE RAGNGIHGGG SITAFYTVLT EGDDQQDPIA DSARAILDGH IVLSRRLAEA 

       370        380        390        400        410        420 
GHYPAIDIEA SISRAMTALI TEQHYARVRL FKQLLSSFQR NRDLVSVGAY AKGSDPMLDK 

       430        440        450 
AITLWPQLEA FLQQGIFERA DWEDSLQALD LIFPTV 

« Hide

References

« Hide 'large scale' references
[1]"Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits."
Vogler A.P., Homma M., Irikura V.M., Macnab R.M.
J. Bacteriol. 173:3564-3572(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"Genetic and biochemical analysis of Salmonella typhimurium FliI, a flagellar protein related to the catalytic subunit of the F0F1 ATPase and to virulence proteins of mammalian and plant pathogens."
Dreyfus G., Williams A.W., Kawagishi I., Macnab R.M.
J. Bacteriol. 175:3131-3138(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62408 Genomic DNA. Translation: AAA27101.1.
AE006468 Genomic DNA. Translation: AAL20884.1.
PIRC42364.
RefSeqNP_460925.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DPYX-ray2.40A/B19-456[»]
ProteinModelPortalP26465.
SMRP26465. Positions 23-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59076N.
IntActP26465. 1 interaction.
STRING99287.STM1972.

Protein family/group databases

TCDB3.A.6.2.1. the type iii (virulence-related) secretory pathway (iiisp) family.

Proteomic databases

PaxDbP26465.
PRIDEP26465.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20884; AAL20884; STM1972.
GeneID1253493.
KEGGstm:STM1972.
PATRIC32382507. VBISalEnt20916_2089.

Phylogenomic databases

eggNOGCOG1157.
HOGENOMHOG000257876.
KOK02412.
OMANDDSYHP.
OrthoDBEOG6W9X53.
ProtClustDBPRK07960.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1982-MONOMER.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR005714. ATPase_T3SS_FliI/YscN.
IPR020005. FliI_clade1.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR15184:SF9. PTHR15184:SF9. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR03496. FliI_clade1. 1 hit.
TIGR01026. fliI_yscN. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26465.

Entry information

Entry nameFLII_SALTY
AccessionPrimary (citable) accession number: P26465
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 13, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references