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Entry version 109 (23 Feb 2022)
Sequence version 1 (01 Oct 1996)
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Protein

Flotillin-like protein FloA

Gene

floA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352).

Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial; in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentation including sporulation, biofilm formation and DNA uptake competence (PubMed:25909364).

Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined (PubMed:27362352).

Involved in spatial organization of membranes, perhaps recruiting proteins to specific membrane regions (PubMed:23651456).

Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings (PubMed:24222488).

1 Publication6 Publications

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU25380-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Flotillin-like protein FloA1 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:floA1 PublicationUniRule annotation
Synonyms:yqfA
Ordered Locus Names:BSU25380
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei6 – 26HelicalUniRule annotationAdd BLAST21
Transmembranei28 – 48HelicalUniRule annotationAdd BLAST21

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

No effect on KinC activity, a double floT-floA deletion decreases the number of proteins in the DRM, blocks the ability of KinC to stimulate biofilm formation (PubMed:20713508). Single floA deletion has no change in FloT localization. Double floA-floT mutants have marked defects in cell morphology, motility, and transformation efficiency (PubMed:22753055). Single floA deletion sporulates less well. Double floA-floT deletion makes no biofilm, has greatly reduced FtsH, sporulates less than either single mutant (PubMed:22882210). Single mutation has a decrease in membrane fluidity, 25% decrease in protein secretion, double floT-floA deletion a stronger decrease in membrane fluidity and 35% decrease in protein secretion (PubMed:23651456). Double floA-floT deletion has reduced oligomerization of KinC (PubMed:26297017). Double floA-floT deletion cells are somewhat elongated, the site of cell wall synthesis is affected, increasing at division septa. The speed of MreB movement around the cell is significantly decreased in rich medium (PubMed:32662773).6 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi240 – 242AEA → GLG: No longer homooligomerizes, poor aggregation, severe decrease in the number of foci. 1 Publication3
Mutagenesisi251 – 253AEE → GLL: No longer homooligomerizes, poor aggregation, severe decrease in the number of foci. 1 Publication3
Mutagenesisi278 – 282EAEAE → LGLGL: Homooligomerizes, no change in number of foci. 1 Publication5
Mutagenesisi288 – 290AEA → GLG: No longer homooligomerizes, poor aggregation, severe decrease in the number of foci. Protein is dispersed in the cell membrane. 1 Publication3

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000497931 – 331Flotillin-like protein FloAAdd BLAST331

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P54466

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P54466

PRoteomics IDEntifications database

More...
PRIDEi
P54466

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Few foci are seen on rich media, when cells are grown in minimal medium more foci are seen (at protein level) (PubMed:22753055). Constitutively expressed in rich and sporulation/biofilm-inducing media, not controlled by spo0A (at protein level) (PubMed:25909364).2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooligomerizes (PubMed:25909364).

Interacts with FloT (PubMed:23651456, PubMed:25909364, PubMed:26297017).

Interacts with FtsH midcell (Probable).

Interacts with PhoR, colocalizes with PhoR in FloA-only membrane rafts (PubMed:25909364).

1 Publication3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU25380

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P54466

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni236 – 331Required for correct localization1 PublicationAdd BLAST96
Regioni312 – 331DisorderedSequence analysisAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi240 – 242EA repeat 11 Publication3
Motifi251 – 253EA repeat 21 Publication3
Motifi278 – 282EA repeat 31 Publication5
Motifi288 – 290EA repeat 41 Publication3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The last 95 residues are required for correct localization (PubMed:22753055). The C-terminus determines the oligomerization state of the protein; there are many small foci for FloA. Swapping with the C-terminus of FloT leads to fewer large foci (PubMed:25909364). N-terminally tagged, purified protein lacking the first 10 residues oligomerizes, with 12mer to about 50mer complexes found (PubMed:27362352).3 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the flotillin-like FloA family.UniRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG4864, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P54466

Identification of Orthologs from Complete Genome Data

More...
OMAi
GIMDYYR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P54466

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01562, FloA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022853, Uncharacterised_YdfA-immunity

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12127, YdfA_immunity, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P54466-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDPSTLMILA IVAVAIIVLA VFFTFVPVML WISALAAGVK ISIFTLVGMR
60 70 80 90 100
LRRVIPNRVV NPLIKAHKAG LNVGTNQLES HYLAGGNVDR VVNALIAAQR
110 120 130 140 150
ANIELTFERC AAIDLAGRDV LEAVQMSVNP KVIETPFIAG VAMDGIEVKA
160 170 180 190 200
KARITVRANI ERLVGGAGEE TIVARVGEGI VSTIGSSDNH KKVLENPDMI
210 220 230 240 250
SQTVLGKGLD SGTAFEILSI DIADVDIGKN IGAILQTDQA EADKNIAQAK
260 270 280 290 300
AEERRAMAVA QEQEMRARVE EMRAKVVEAE AEVPLAMAEA LREGNIGVMD
310 320 330
YMNIKNIDAD TEMRDSFGKL TKDPSDEDRK S
Length:331
Mass (Da):35,641
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i484AD959F8109A7A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D84432 Genomic DNA Translation: BAA12473.1
AL009126 Genomic DNA Translation: CAB14480.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A69953

NCBI Reference Sequences

More...
RefSeqi
NP_390416.1, NC_000964.3
WP_003230026.1, NZ_JNCM01000036.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB14480; CAB14480; BSU_25380

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
937865

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU25380

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.2759

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84432 Genomic DNA Translation: BAA12473.1
AL009126 Genomic DNA Translation: CAB14480.1
PIRiA69953
RefSeqiNP_390416.1, NC_000964.3
WP_003230026.1, NZ_JNCM01000036.1

3D structure databases

SMRiP54466
ModBaseiSearch...

Protein-protein interaction databases

STRINGi224308.BSU25380

Proteomic databases

jPOSTiP54466
PaxDbiP54466
PRIDEiP54466

Genome annotation databases

EnsemblBacteriaiCAB14480; CAB14480; BSU_25380
GeneIDi937865
KEGGibsu:BSU25380
PATRICifig|224308.179.peg.2759

Phylogenomic databases

eggNOGiCOG4864, Bacteria
InParanoidiP54466
OMAiGIMDYYR
PhylomeDBiP54466

Enzyme and pathway databases

BioCyciBSUB:BSU25380-MONOMER

Family and domain databases

HAMAPiMF_01562, FloA, 1 hit
InterProiView protein in InterPro
IPR022853, Uncharacterised_YdfA-immunity
PfamiView protein in Pfam
PF12127, YdfA_immunity, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFLOA_BACSU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P54466
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 23, 2022
This is version 109 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  2. SIMILARITY comments
    Index of protein domains and families
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