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Protein

Flagellar M-ring protein

Gene

fliF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The M ring may be actively involved in energy transduction.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:FLIF-FLAGELLAR-MS-RING.
ECOL316407:JW1922-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flagellar M-ring protein
Gene namesi
Name:fliF
Synonyms:fla AII.1, fla BI
Ordered Locus Names:b1938, JW1922
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11347. fliF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4321HelicalSequence analysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Bacterial flagellum, Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Flagellar M-ring proteinPRO_0000180882Add
BLAST

Proteomic databases

EPDiP25798.
PaxDbiP25798.
PRIDEiP25798.

Interactioni

Subunit structurei

The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. The M ring is integral to the inner membrane of the cell and may be connected to the flagellar rod via the S ring. The S (supramembrane ring) lies just distal to the M ring. The L and P rings lie in the outer membrane and the periplasmic space, respectively.

Binary interactionsi

WithEntry#Exp.IntActNotes
fliGP0ABZ14EBI-1126492,EBI-1126524

Protein-protein interaction databases

BioGridi4260383. 4 interactions.
DIPiDIP-401N.
IntActiP25798. 4 interactions.
STRINGi511145.b1938.

Structurei

3D structure databases

ProteinModelPortaliP25798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FliF family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C1F. Bacteria.
COG1766. LUCA.
HOGENOMiHOG000265848.
InParanoidiP25798.
KOiK02409.
OMAiNFQRGLE.
OrthoDBiEOG6KMB3J.
PhylomeDBiP25798.

Family and domain databases

InterProiIPR013556. Flag_M-ring_C.
IPR000067. FlgMring_FliF.
IPR006182. YscJ_FliF.
[Graphical view]
PfamiPF01514. YscJ_FliF. 1 hit.
PF08345. YscJ_FliF_C. 1 hit.
[Graphical view]
PIRSFiPIRSF004862. FliF. 1 hit.
PRINTSiPR01009. FLGMRINGFLIF.
TIGRFAMsiTIGR00206. fliF. 1 hit.

Sequencei

Sequence statusi: Complete.

P25798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNATAAQTKS LEWLNRLRAN PKIPLIVAGS AAVAVMVALI LWAKAPDYRT
60 70 80 90 100
LFSNLSDQDG GAIVSQLTQM NIPYRFSEAS GAIEVPADKV HELRLRLAQQ
110 120 130 140 150
GLPKGGAVGF ELLDQEKFGI SQFSEQVNYQ RALEGELSRT IETIGPVKGA
160 170 180 190 200
RVHLAMPKPS LFVREQKSPS ASVTVNLLPG RALDEGQISA IVHLVSSAVA
210 220 230 240 250
GLPPGNVTLV DQGGHLLTQS NTSGRDLNDA QLKYASDVEG RIQRRIEAIL
260 270 280 290 300
SPIVGNGNIH AQVTAQLDFA SKEQTEEQYR PNGDESHAAL RSRQLNESEQ
310 320 330 340 350
SGSGYPGGVP GALSNQPAPA NNAPISTPPA NQNNRQQQAS TTSNSGPRST
360 370 380 390 400
QRNETSNYEV DRTIRHTKMN VGDVQRLSVA VVVNYKTLPD GKPLPLSNEQ
410 420 430 440 450
MKQIEDLTRE AMGFSEKRGD SLNVVNSPFN SSDESGGELP FWQQQAFIDQ
460 470 480 490 500
LLAAGRWLLV LLVAWLLWRK AVRPQLTRRA EAMKAVQQQA QAREEVEDAV
510 520 530 540 550
EVRLSKDEQL QQRRANQRLG AEVMSQRIRE MSDNDPRVVA LVIRQWINND

HE
Length:552
Mass (Da):60,589
Last modified:November 1, 1997 - v3
Checksum:iB2038FDBEA914DA5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601H → R in BAA14029 (Ref. 1) Curated
Sequence conflicti266 – 2661Q → H in BAA14029 (Ref. 1) Curated
Sequence conflicti541 – 5411L → V (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89826 Genomic DNA. Translation: BAA14029.1.
U00096 Genomic DNA. Translation: AAC75005.1.
AP009048 Genomic DNA. Translation: BAA15763.1.
M84992 Genomic DNA. No translation available.
L13243 Genomic DNA. No translation available.
PIRiG64957.
RefSeqiNP_416448.1. NC_000913.3.
WP_000994427.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75005; AAC75005; b1938.
BAA15763; BAA15763; BAA15763.
GeneIDi946448.
KEGGiecj:JW1922.
eco:b1938.
PATRICi32119205. VBIEscCol129921_2017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89826 Genomic DNA. Translation: BAA14029.1.
U00096 Genomic DNA. Translation: AAC75005.1.
AP009048 Genomic DNA. Translation: BAA15763.1.
M84992 Genomic DNA. No translation available.
L13243 Genomic DNA. No translation available.
PIRiG64957.
RefSeqiNP_416448.1. NC_000913.3.
WP_000994427.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP25798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260383. 4 interactions.
DIPiDIP-401N.
IntActiP25798. 4 interactions.
STRINGi511145.b1938.

Proteomic databases

EPDiP25798.
PaxDbiP25798.
PRIDEiP25798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75005; AAC75005; b1938.
BAA15763; BAA15763; BAA15763.
GeneIDi946448.
KEGGiecj:JW1922.
eco:b1938.
PATRICi32119205. VBIEscCol129921_2017.

Organism-specific databases

EchoBASEiEB1323.
EcoGeneiEG11347. fliF.

Phylogenomic databases

eggNOGiENOG4105C1F. Bacteria.
COG1766. LUCA.
HOGENOMiHOG000265848.
InParanoidiP25798.
KOiK02409.
OMAiNFQRGLE.
OrthoDBiEOG6KMB3J.
PhylomeDBiP25798.

Enzyme and pathway databases

BioCyciEcoCyc:FLIF-FLAGELLAR-MS-RING.
ECOL316407:JW1922-MONOMER.

Miscellaneous databases

PROiP25798.

Family and domain databases

InterProiIPR013556. Flag_M-ring_C.
IPR000067. FlgMring_FliF.
IPR006182. YscJ_FliF.
[Graphical view]
PfamiPF01514. YscJ_FliF. 1 hit.
PF08345. YscJ_FliF_C. 1 hit.
[Graphical view]
PIRSFiPIRSF004862. FliF. 1 hit.
PRINTSiPR01009. FLGMRINGFLIF.
TIGRFAMsiTIGR00206. fliF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. al Mamun A.A.M., Tominaga A., Enomoto M.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Characterization of the fliE genes of Escherichia coli and Salmonella typhimurium and identification of the FliE protein as a component of the flagellar hook-basal body complex."
    Mueller V., Jones C.J., Kawagishi I., Aizawa S., Macnab R.M.
    J. Bacteriol. 174:2298-2304(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
    Strain: JA11.
  6. "Gene sequence, overproduction, purification and determination of the wild-type level of the Escherichia coli flagellar switch protein FliG."
    Roman S.J., Frantz B.B., Matsumura P.
    Gene 133:103-108(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 532-552.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiFLIF_ECOLI
AccessioniPrimary (citable) accession number: P25798
Secondary accession number(s): P76324, P76914
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: November 1, 1997
Last modified: March 16, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.