FLOA_BACSU
ID FLOA_BACSU Reviewed; 331 AA.
AC P54466;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Flotillin-like protein FloA {ECO:0000255|HAMAP-Rule:MF_01562, ECO:0000303|PubMed:22753055};
GN Name=floA {ECO:0000255|HAMAP-Rule:MF_01562, ECO:0000303|PubMed:22753055};
GN Synonyms=yqfA; OrderedLocusNames=BSU25380;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=22753055; DOI=10.1128/jb.00910-12;
RA Dempwolff F., Moeller H.M., Graumann P.L.;
RT "Synthetic motility and cell shape defects associated with deletions of
RT flotillin/reggie paralogs in Bacillus subtilis and interplay of these
RT proteins with NfeD proteins.";
RL J. Bacteriol. 194:4652-4661(2012).
RN [5]
RP INTERACTION WITH FTSH, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [6]
RP FUNCTION, INTERACTION WITH FLOT, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [7]
RP FUNCTION IN CELL DIVISION, AND FUNCTION IN DIFFERENTIATION.
RC STRAIN=168 / PY79;
RX PubMed=24222488; DOI=10.1128/mbio.00719-13;
RA Mielich-Suess B., Schneider J., Lopez D.;
RT "Overproduction of flotillin influences cell differentiation and shape in
RT Bacillus subtilis.";
RL MBio 4:0-0(2013).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH PHOR, SUBCELLULAR LOCATION, INDUCTION,
RP DOMAIN, AND MUTAGENESIS OF 240-ALA--ALA-242; 251-ALA--GLU-253;
RP 278-GLU--GLU-282 AND 288-ALA--ALA-290.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=25909364; DOI=10.1371/journal.pgen.1005140;
RA Schneider J., Klein T., Mielich-Suess B., Koch G., Franke C., Kuipers O.P.,
RA Kovacs A.T., Sauer M., Lopez D.;
RT "Spatio-temporal remodeling of functional membrane microdomains organizes
RT the signaling networks of a bacterium.";
RL PLoS Genet. 11:e1005140-e1005140(2015).
RN [9]
RP INTERACTION WITH FLOT, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=26297017; DOI=10.1099/mic.0.000137;
RA Schneider J., Mielich-Suess B., Boehme R., Lopez D.;
RT "In vivo characterization of the scaffold activity of flotillin on the
RT membrane kinase KinC of Bacillus subtilis.";
RL Microbiology 161:1871-1887(2015).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=168, and 168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=32662773; DOI=10.7554/elife.57179;
RA Zielinska A., Savietto A., de Sousa Borges A., Martinez D., Berbon M.,
RA Roelofsen J.R., Hartman A.M., de Boer R., Van der Klei I.J., Hirsch A.K.,
RA Habenstein B., Bramkamp M., Scheffers D.J.;
RT "Flotillin-mediated membrane fluidity controls peptidoglycan synthesis and
RT MreB movement.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Found in functional membrane microdomains (FMM) that may be
CC equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and
CC increase in number as cells age. FloA and FloT function is partially
CC redundant; double deletions have marked synthetic phenotypes
CC (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352).
CC Flotillins are thought to be important factors in membrane fluidity,
CC especially during periods of rapid growth in rich media (Probable).
CC Whether specific proteins are associated with FMMs is controversial; in
CC one study FloT rafts have been shown to include proteins involved in
CC adaptation to stationary phase, while FloA-FloT rafts include proteins
CC involved in differentation including sporulation, biofilm formation and
CC DNA uptake competence (PubMed:25909364). Another (more finely resolved)
CC study only showed association of NfeD2 with FloT rafts of all the
CC proteins examined (PubMed:27362352). Involved in spatial organization
CC of membranes, perhaps recruiting proteins to specific membrane regions
CC (PubMed:23651456). Simultaneous overexpression of both FloA and FloT
CC leads to defects in cell division and differentiation, in part caused
CC by stabilization of FtsH and its subsequent increased ability to
CC degrade proteins. Cells make more biofilm, are about half as long, have
CC less EzrA and more frequent Z-rings (PubMed:24222488).
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:24222488,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:32662773}.
CC -!- SUBUNIT: Homooligomerizes (PubMed:25909364). Interacts with FloT
CC (PubMed:23651456, PubMed:25909364, PubMed:26297017). Interacts with
CC FtsH midcell (Probable). Interacts with PhoR, colocalizes with PhoR in
CC FloA-only membrane rafts (PubMed:25909364).
CC {ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364,
CC ECO:0000269|PubMed:26297017, ECO:0000305|PubMed:22882210}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01562,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:20713508, ECO:0000305|PubMed:22753055}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_01562}. Membrane raft
CC {ECO:0000255|HAMAP-Rule:MF_01562, ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:23651456}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01562}. Note=Present in detergent-resistant
CC membrane (DRM) fractions, approximately 6 dynamic foci per cell;
CC sometimes colocalizes with FloT in DRMs (PubMed:20713508,
CC PubMed:22882210, PubMed:23651456). Found in discrete, highly mobile
CC foci, rarely colocalizes with FloT (PubMed:22753055). At the septa
CC colocalizes with FloT and FtsH (PubMed:22882210). Careful analysis
CC gives an average of 13 FloA and 6 FloT foci per cell; FloA foci are
CC smaller that FloT foci (PubMed:25909364). Another study shows FloA and
CC FloT foci are similar in size, forming membrane assemblies of 85-110
CC nm, but FloA are more mobile than FloT foci. This study found no
CC evidence of colocalization of FloA with FloT (PubMed:27362352).
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}.
CC -!- INDUCTION: Few foci are seen on rich media, when cells are grown in
CC minimal medium more foci are seen (at protein level) (PubMed:22753055).
CC Constitutively expressed in rich and sporulation/biofilm-inducing
CC media, not controlled by spo0A (at protein level) (PubMed:25909364).
CC {ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:25909364}.
CC -!- DOMAIN: The last 95 residues are required for correct localization
CC (PubMed:22753055). The C-terminus determines the oligomerization state
CC of the protein; there are many small foci for FloA. Swapping with the
CC C-terminus of FloT leads to fewer large foci (PubMed:25909364). N-
CC terminally tagged, purified protein lacking the first 10 residues
CC oligomerizes, with 12mer to about 50mer complexes found
CC (PubMed:27362352). {ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}.
CC -!- DISRUPTION PHENOTYPE: No effect on KinC activity, a double floT-floA
CC deletion decreases the number of proteins in the DRM, blocks the
CC ability of KinC to stimulate biofilm formation (PubMed:20713508).
CC Single floA deletion has no change in FloT localization. Double floA-
CC floT mutants have marked defects in cell morphology, motility, and
CC transformation efficiency (PubMed:22753055). Single floA deletion
CC sporulates less well. Double floA-floT deletion makes no biofilm, has
CC greatly reduced FtsH, sporulates less than either single mutant
CC (PubMed:22882210). Single mutation has a decrease in membrane fluidity,
CC 25% decrease in protein secretion, double floT-floA deletion a stronger
CC decrease in membrane fluidity and 35% decrease in protein secretion
CC (PubMed:23651456). Double floA-floT deletion has reduced
CC oligomerization of KinC (PubMed:26297017). Double floA-floT deletion
CC cells are somewhat elongated, the site of cell wall synthesis is
CC affected, increasing at division septa. The speed of MreB movement
CC around the cell is significantly decreased in rich medium
CC (PubMed:32662773). {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:26297017,
CC ECO:0000269|PubMed:32662773}.
CC -!- SIMILARITY: Belongs to the flotillin-like FloA family.
CC {ECO:0000255|HAMAP-Rule:MF_01562}.
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DR EMBL; D84432; BAA12473.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14480.1; -; Genomic_DNA.
DR PIR; A69953; A69953.
DR RefSeq; NP_390416.1; NC_000964.3.
DR RefSeq; WP_003230026.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54466; -.
DR SMR; P54466; -.
DR STRING; 224308.BSU25380; -.
DR jPOST; P54466; -.
DR PaxDb; P54466; -.
DR PRIDE; P54466; -.
DR EnsemblBacteria; CAB14480; CAB14480; BSU_25380.
DR GeneID; 937865; -.
DR KEGG; bsu:BSU25380; -.
DR PATRIC; fig|224308.179.peg.2759; -.
DR eggNOG; COG4864; Bacteria.
DR InParanoid; P54466; -.
DR OMA; GIMDYYR; -.
DR PhylomeDB; P54466; -.
DR BioCyc; BSUB:BSU25380-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_01562; FloA; 1.
DR InterPro; IPR022853; FloA.
DR Pfam; PF12127; YdfA_immunity; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..331
FT /note="Flotillin-like protein FloA"
FT /id="PRO_0000049793"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01562"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01562"
FT REGION 236..331
FT /note="Required for correct localization"
FT /evidence="ECO:0000269|PubMed:22753055"
FT REGION 312..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..242
FT /note="EA repeat 1"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MOTIF 251..253
FT /note="EA repeat 2"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MOTIF 278..282
FT /note="EA repeat 3"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MOTIF 288..290
FT /note="EA repeat 4"
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 240..242
FT /note="AEA->GLG: No longer homooligomerizes, poor
FT aggregation, severe decrease in the number of foci."
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 251..253
FT /note="AEE->GLL: No longer homooligomerizes, poor
FT aggregation, severe decrease in the number of foci."
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 278..282
FT /note="EAEAE->LGLGL: Homooligomerizes, no change in number
FT of foci."
FT /evidence="ECO:0000269|PubMed:25909364"
FT MUTAGEN 288..290
FT /note="AEA->GLG: No longer homooligomerizes, poor
FT aggregation, severe decrease in the number of foci. Protein
FT is dispersed in the cell membrane."
FT /evidence="ECO:0000269|PubMed:25909364"
SQ SEQUENCE 331 AA; 35641 MW; 484AD959F8109A7A CRC64;
MDPSTLMILA IVAVAIIVLA VFFTFVPVML WISALAAGVK ISIFTLVGMR LRRVIPNRVV
NPLIKAHKAG LNVGTNQLES HYLAGGNVDR VVNALIAAQR ANIELTFERC AAIDLAGRDV
LEAVQMSVNP KVIETPFIAG VAMDGIEVKA KARITVRANI ERLVGGAGEE TIVARVGEGI
VSTIGSSDNH KKVLENPDMI SQTVLGKGLD SGTAFEILSI DIADVDIGKN IGAILQTDQA
EADKNIAQAK AEERRAMAVA QEQEMRARVE EMRAKVVEAE AEVPLAMAEA LREGNIGVMD
YMNIKNIDAD TEMRDSFGKL TKDPSDEDRK S
