NFED2_BACSU
ID NFED2_BACSU Reviewed; 174 AA.
AC O32077;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Membrane protein NfeD2 {ECO:0000303|PubMed:22753055};
GN Name=nfeD2 {ECO:0000303|PubMed:22753055}; Synonyms=yuaF;
GN OrderedLocusNames=BSU31020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=11454200; DOI=10.1046/j.1365-2958.2001.02489.x;
RA Wiegert T., Homuth G., Versteeg S., Schumann W.;
RT "Alkaline shock induces the Bacillus subtilis sigma(W) regulon.";
RL Mol. Microbiol. 41:59-71(2001).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION 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 [4]
RP SUBCELLULAR LOCATION.
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 [5]
RP COLOCALIZATION WITH FLOT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [6]
RP STRUCTURE BY NMR OF 97-174.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=18696230; DOI=10.1007/s10858-008-9261-3;
RA Walker C.A., Hinderhofer M., Witte D.J., Boos W., Moeller H.M.;
RT "Solution structure of the soluble domain of the NfeD protein YuaF from
RT Bacillus subtilis.";
RL J. Biomol. NMR 42:69-76(2008).
CC -!- FUNCTION: Plays a role in assembly of FloT membrane rafts, probably
CC recruited to rafts by FloT. {ECO:0000269|PubMed:22753055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:22753055, ECO:0000305|PubMed:24222488}; Multi-pass
CC membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:27362352,
CC ECO:0000305|PubMed:24222488}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Found in discrete, highly mobile foci, often
CC colocalizes with FloT (PubMed:22753055, PubMed:24222488). Localization
CC in membrane rafts requires floT (PubMed:22753055). Another study also
CC shows colocalization with FloT; membrane assemblies of NfeD2 are
CC slightly larger than FloT membrane assemblies (PubMed:27362352).
CC {ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:24222488,
CC ECO:0000269|PubMed:27362352}.
CC -!- INDUCTION: Expression is sigma W-dependent. Up-regulated by alkali
CC shock and by infection with phage SPP1. {ECO:0000269|PubMed:11454200}.
CC -!- DISRUPTION PHENOTYPE: Alters assembly of FloT membrane rafts; more
CC diffuse rafts are seen. Double floA-nfeD2 deletion mutants are wild-
CC type (PubMed:22753055). No visible effect on FloT membrane assemblies
CC (PubMed:27362352). {ECO:0000269|PubMed:22753055,
CC ECO:0000269|PubMed:27362352}.
CC -!- SIMILARITY: Belongs to the NfeD family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15080.1; -; Genomic_DNA.
DR PIR; H70005; H70005.
DR RefSeq; NP_390980.1; NC_000964.3.
DR RefSeq; WP_003243808.1; NZ_JNCM01000033.1.
DR PDB; 2K14; NMR; -; A=97-174.
DR PDBsum; 2K14; -.
DR AlphaFoldDB; O32077; -.
DR BMRB; O32077; -.
DR SMR; O32077; -.
DR STRING; 224308.BSU31020; -.
DR PaxDb; O32077; -.
DR EnsemblBacteria; CAB15080; CAB15080; BSU_31020.
DR GeneID; 937144; -.
DR KEGG; bsu:BSU31020; -.
DR PATRIC; fig|224308.179.peg.3362; -.
DR eggNOG; COG1585; Bacteria.
DR OMA; AGNTIHT; -.
DR BioCyc; BSUB:BSU31020-MON; -.
DR EvolutionaryTrace; O32077; -.
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 Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..174
FT /note="Membrane protein NfeD2"
FT /id="PRO_0000379129"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:2K14"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2K14"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2K14"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:2K14"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2K14"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2K14"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2K14"
SQ SEQUENCE 174 AA; 18604 MW; 86B59CE347A61F31 CRC64;
MELFGVPIQT MYLYTLIIAG SLTLLFLFFG DVFSGLSEGI PFLNPTLVLS FFTCFSAGGY
IGELVLPLSS LLIALLSCIL SIMLVVLLHI FVLVPLSSAE ESLAYREDDL RGRLGKVITA
VPVDGFGEVV IEGIGGTISK SAVSFDNQQI SYGTTVLVVD INNGVLSVTP HEPI
