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Protein

Flagellar M-ring protein

Gene

fliF

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 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

BioCyciSENT99287:GCTI-1979-MONOMER.

Protein family/group databases

TCDBi3.A.6.2.1. the type iii (virulence-related) secretory pathway (iiisp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Flagellar M-ring protein
Gene namesi
Name:fliF
Synonyms:fla AII.1, fla BI
Ordered Locus Names:STM1969
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei26 – 4621HelicalSequence analysisAdd
BLAST
Transmembranei455 – 47521HelicalSequence 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
Initiator methionineiRemoved
Chaini2 – 560559Flagellar M-ring proteinPRO_0000180883Add
BLAST

Proteomic databases

PaxDbiP15928.
PRIDEiP15928.

Expressioni

Inductioni

Inhibited in nutrient-poor medium.1 Publication

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
fliGP0A1J94EBI-2012119,EBI-2012130

Protein-protein interaction databases

IntActiP15928. 2 interactions.
STRINGi99287.STM1969.

Structurei

3D structure databases

ProteinModelPortaliP15928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FliF family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C1F. Bacteria.
COG1766. LUCA.
HOGENOMiHOG000265848.
KOiK02409.
OMAiNFQRGLE.
PhylomeDBiP15928.

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.

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

P15928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATASTATQ PKPLEWLNRL RANPRIPLIV AGSAAVAIVV AMVLWAKTPD
60 70 80 90 100
YRTLFSNLSD QDGGAIVAQL TQMNIPYRFA NGSGAIEVPA DKVHELRLRL
110 120 130 140 150
AQQGLPKGGA VGFELLDQEK FGISQFSEQV NYQRALEGEL ARTIETLGPV
160 170 180 190 200
KSARVHLAMP KPSLFVREQK SPSASVTVTL EPGRALDEGQ ISAVVHLVSS
210 220 230 240 250
AVAGLPPGNV TLVDQSGHLL TQSNTSGRDL NDAQLKFAND VESRIQRRIE
260 270 280 290 300
AILSPIVGNG NVHAQVTAQL DFANKEQTEE HYSPNGDASK ATLRSRQLNI
310 320 330 340 350
SEQVGAGYPG GVPGALSNQP APPNEAPIAT PPTNQQNAQN TPQTSTSTNS
360 370 380 390 400
NSAGPRSTQR NETSNYEVDR TIRHTKMNVG DIERLSVAVV VNYKTLADGK
410 420 430 440 450
PLPLTADQMK QIEDLTREAM GFSDKRGDTL NVVNSPFSAV DNTGGELPFW
460 470 480 490 500
QQQSFIDQLL AAGRWLLVLV VAWILWRKAV RPQLTRRVEE AKAAQEQAQV
510 520 530 540 550
RQETEEAVEV RLSKDEQLQQ RRANQRLGAE VMSQRIREMS DNDPRVVALV
560
IRQWMSNDHE
Length:560
Mass (Da):61,230
Last modified:January 23, 2007 - v2
Checksum:i7A5011F4EF17B488
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24462 Genomic DNA. Translation: AAA27096.1.
AE006468 Genomic DNA. Translation: AAL20881.1.
M84993 Genomic DNA. Translation: AAA27094.1.
PIRiC32887. D30930.
RefSeqiNP_460922.1. NC_003197.1.
WP_001276834.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20881; AAL20881; STM1969.
GeneIDi1253490.
KEGGistm:STM1969.
PATRICi32382501. VBISalEnt20916_2086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24462 Genomic DNA. Translation: AAA27096.1.
AE006468 Genomic DNA. Translation: AAL20881.1.
M84993 Genomic DNA. Translation: AAA27094.1.
PIRiC32887. D30930.
RefSeqiNP_460922.1. NC_003197.1.
WP_001276834.1. NC_003197.1.

3D structure databases

ProteinModelPortaliP15928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15928. 2 interactions.
STRINGi99287.STM1969.

Protein family/group databases

TCDBi3.A.6.2.1. the type iii (virulence-related) secretory pathway (iiisp) family.

Proteomic databases

PaxDbiP15928.
PRIDEiP15928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20881; AAL20881; STM1969.
GeneIDi1253490.
KEGGistm:STM1969.
PATRICi32382501. VBISalEnt20916_2086.

Phylogenomic databases

eggNOGiENOG4105C1F. Bacteria.
COG1766. LUCA.
HOGENOMiHOG000265848.
KOiK02409.
OMAiNFQRGLE.
PhylomeDBiP15928.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1979-MONOMER.

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...

Entry informationi

Entry nameiFLIF_SALTY
AccessioniPrimary (citable) accession number: P15928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 109 of the entry and version 2 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. 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.