MREB_BACSU
ID MREB_BACSU Reviewed; 337 AA.
AC Q01465;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000305};
DE AltName: Full=Actin-like MreB protein {ECO:0000305};
DE AltName: Full=Rod shape-determining protein MreB {ECO:0000305};
GN Name=mreB; OrderedLocusNames=BSU28030;
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;
RX PubMed=1400225; DOI=10.1128/jb.174.21.6729-6742.1992;
RA Varley A.W., Stewart G.C.;
RT "The divIVB region of the Bacillus subtilis chromosome encodes homologs of
RT Escherichia coli septum placement (minCD) and cell shape (mreBCD)
RT determinants.";
RL J. Bacteriol. 174:6729-6742(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400224; DOI=10.1128/jb.174.21.6717-6728.1992;
RA Levin P.A., Margolis P.S., Setlow P., Losick R., Sun D.;
RT "Identification of Bacillus subtilis genes for septum placement and shape
RT determination.";
RL J. Bacteriol. 174:6717-6728(1992).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 98.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=8387996; DOI=10.1128/jb.175.10.3139-3145.1993;
RA Butler Y.X., Abhayawardhane Y., Stewart G.C.;
RT "Amplification of the Bacillus subtilis maf gene results in arrested septum
RT formation.";
RL J. Bacteriol. 175:3139-3145(1993).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11290328; DOI=10.1016/s0092-8674(01)00287-2;
RA Jones L.J., Carballido-Lopez R., Errington J.;
RT "Control of cell shape in bacteria: helical, actin-like filaments in
RT Bacillus subtilis.";
RL Cell 104:913-922(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14588250; DOI=10.1016/j.cub.2003.10.024;
RA Soufo H.J., Graumann P.L.;
RT "Actin-like proteins MreB and Mbl from Bacillus subtilis are required for
RT bipolar positioning of replication origins.";
RL Curr. Biol. 13:1916-1920(2003).
RN [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15745453; DOI=10.1186/1471-2121-6-10;
RA Defeu Soufo H.J., Graumann P.L.;
RT "Bacillus subtilis actin-like protein MreB influences the positioning of
RT the replication machinery and requires membrane proteins MreC/D and other
RT actin-like proteins for proper localization.";
RL BMC Cell Biol. 6:10-10(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16950129; DOI=10.1016/j.devcel.2006.07.017;
RA Carballido-Lopez R., Formstone A., Li Y., Ehrlich S.D., Noirot P.,
RA Errington J.;
RT "Actin homolog MreBH governs cell morphogenesis by localization of the cell
RT wall hydrolase LytE.";
RL Dev. Cell 11:399-409(2006).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH MBL AND MREBH, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF ASP-158.
RX PubMed=17064365; DOI=10.1111/j.1365-2958.2006.05457.x;
RA Defeu Soufo H.J., Graumann P.L.;
RT "Dynamic localization and interaction with other Bacillus subtilis actin-
RT like proteins are important for the function of MreB.";
RL Mol. Microbiol. 62:1340-1356(2006).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=19117023; DOI=10.1002/cm.20332;
RA Mayer J.A., Amann K.J.;
RT "Assembly properties of the Bacillus subtilis actin, MreB.";
RL Cell Motil. Cytoskeleton 66:109-118(2009).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19659933; DOI=10.1111/j.1365-2958.2009.06805.x;
RA Kawai Y., Asai K., Errington J.;
RT "Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in
RT cell morphogenesis of Bacillus subtilis.";
RL Mol. Microbiol. 73:719-731(2009).
RN [13]
RP FUNCTION.
RX PubMed=21636745; DOI=10.1126/science.1203285;
RA Garner E.C., Bernard R., Wang W., Zhuang X., Rudner D.Z., Mitchison T.;
RT "Coupled, circumferential motions of the cell wall synthesis machinery and
RT MreB filaments in B. subtilis.";
RL Science 333:222-225(2011).
RN [14]
RP FUNCTION.
RX PubMed=21636744; DOI=10.1126/science.1203466;
RA Dominguez-Escobar J., Chastanet A., Crevenna A.H., Fromion V.,
RA Wedlich-Soeldner R., Carballido-Lopez R.;
RT "Processive movement of MreB-associated cell wall biosynthetic complexes in
RT bacteria.";
RL Science 333:225-228(2011).
RN [15]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=23249255; DOI=10.1186/1471-2180-12-298;
RA Dempwolff F., Wischhusen H.M., Specht M., Graumann P.L.;
RT "The deletion of bacterial dynamin and flotillin genes results in
RT pleiotrophic effects on cell division, cell growth and in cell shape
RT maintenance.";
RL BMC Microbiol. 12:298-298(2012).
RN [16]
RP FUNCTION.
RX PubMed=24603761; DOI=10.1038/ncomms4442;
RA Strahl H., Buermann F., Hamoen L.W.;
RT "The actin homologue MreB organizes the bacterial cell membrane.";
RL Nat. Commun. 5:3442-3442(2014).
RN [17]
RP FUNCTION.
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: Forms membrane-associated dynamic filaments that are
CC essential for cell shape determination (PubMed:11290328,
CC PubMed:15745453, PubMed:17064365, PubMed:19117023, PubMed:19659933).
CC Acts by regulating cell wall synthesis and cell elongation, and thus
CC cell shape (PubMed:19659933). A feedback loop between cell geometry and
CC MreB localization may maintain elongated cell shape by targeting cell
CC wall growth to regions of negative cell wall curvature (By similarity).
CC Filaments rotate around the cell circumference in concert with the cell
CC wall synthesis enzymes. The process is driven by the cell wall
CC synthesis machinery and does not depend on MreB polymerization
CC (PubMed:21636745, PubMed:21636744). The active movement of the MreB
CC cytoskeleton stimulates diffusion of membrane proteins
CC (PubMed:24603761). Organizes peptidoglycan synthesis in the lateral
CC cell wall (PubMed:19659933). Also required for proper chromosome
CC segregation (PubMed:14588250, PubMed:15745453, PubMed:17064365).
CC Membrane fluidity influences MreB movement; in rich medium MreB
CC movement is significantly decreased in a floA-floT mutant
CC (PubMed:32662773). {ECO:0000250|UniProtKB:P0A9X4,
CC ECO:0000269|PubMed:11290328, ECO:0000269|PubMed:14588250,
CC ECO:0000269|PubMed:15745453, ECO:0000269|PubMed:17064365,
CC ECO:0000269|PubMed:19117023, ECO:0000269|PubMed:19659933,
CC ECO:0000269|PubMed:21636744, ECO:0000269|PubMed:21636745,
CC ECO:0000269|PubMed:24603761, ECO:0000269|PubMed:32662773}.
CC -!- ACTIVITY REGULATION: Polymerizes in the presence of millimolar divalent
CC cations in a protein concentration-dependent manner. Polymerization is
CC favored by decreasing pH and inhibited by monovalent salts and low
CC temperatures. {ECO:0000269|PubMed:19117023}.
CC -!- SUBUNIT: Forms polymers (PubMed:11290328, PubMed:15745453,
CC PubMed:17064365, PubMed:19117023). Forms a complex with Mbl and MreBH
CC (PubMed:17064365, PubMed:19659933). {ECO:0000269|PubMed:11290328,
CC ECO:0000269|PubMed:15745453, ECO:0000269|PubMed:17064365,
CC ECO:0000269|PubMed:19117023, ECO:0000269|PubMed:19659933}.
CC -!- INTERACTION:
CC Q01465; P33166: tuf; NbExp=6; IntAct=EBI-6406749, EBI-2122675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11290328}.
CC Note=Membrane-associated (PubMed:15745453, PubMed:17064365). Localizes
CC in the form of helical filaments that encircle the cell
CC (PubMed:11290328, PubMed:15745453). Localization is affected by Mbl,
CC MreBH, MreC and MreD (PubMed:15745453). Colocalizes with MreBH and Mbl
CC (PubMed:16950129, PubMed:17064365). {ECO:0000269|PubMed:11290328,
CC ECO:0000269|PubMed:15745453, ECO:0000269|PubMed:16950129,
CC ECO:0000269|PubMed:17064365}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene results in loss of cell
CC width control (PubMed:11290328). Depletion leads to a strong defect in
CC chromosome segregation (PubMed:14588250, PubMed:15745453). It also
CC leads to the formation of enlarged cells, to the loss of mid cell
CC localization of the replication machinery and to growth arrest
CC (PubMed:15745453). Double dynA-mreB deletions have strong cell shape
CC defects (PubMed:23249255). {ECO:0000269|PubMed:11290328,
CC ECO:0000269|PubMed:14588250, ECO:0000269|PubMed:15745453,
CC ECO:0000269|PubMed:23249255}.
CC -!- MISCELLANEOUS: B.subtilis has three MreB paralogs: MreB, Mbl and MreBH.
CC All paralogs have the ability to support rod-shaped cell growth normal
CC conditions. The multiplicity of paralogs becomes important under stress
CC conditions. They are probably used to allow cells to maintain proper
CC growth and morphogenesis under changing conditions.
CC {ECO:0000269|PubMed:19659933}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02207, ECO:0000305}.
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DR EMBL; M95582; AAA22605.1; -; Genomic_DNA.
DR EMBL; M96343; AAA22397.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14763.2; -; Genomic_DNA.
DR EMBL; L08793; AAA22584.1; -; Genomic_DNA.
DR PIR; D69660; D69660.
DR RefSeq; NP_390681.2; NC_000964.3.
DR RefSeq; WP_003229650.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; Q01465; -.
DR SMR; Q01465; -.
DR DIP; DIP-58539N; -.
DR IntAct; Q01465; 11.
DR STRING; 224308.BSU28030; -.
DR TCDB; 9.B.157.1.1; the cell shape-determining mrebcd (mrebcd) family.
DR jPOST; Q01465; -.
DR PaxDb; Q01465; -.
DR PRIDE; Q01465; -.
DR EnsemblBacteria; CAB14763; CAB14763; BSU_28030.
DR GeneID; 936759; -.
DR KEGG; bsu:BSU28030; -.
DR PATRIC; fig|224308.179.peg.3045; -.
DR eggNOG; COG1077; Bacteria.
DR InParanoid; Q01465; -.
DR OMA; MVICIPS; -.
DR PhylomeDB; Q01465; -.
DR BioCyc; BSUB:BSU28030-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd10225; MreB_like; 1.
DR HAMAP; MF_02207; MreB; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004753; MreB.
DR PRINTS; PR01652; SHAPEPROTEIN.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00904; mreB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell shape; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..337
FT /note="Cell shape-determining protein MreB"
FT /id="PRO_0000062758"
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 161..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 209..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 289..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT MUTAGEN 158
FT /note="D->A: Causes a severe defect in cell morphology and
FT in chromosome segregation. Can still form filamentous
FT structures, but these are rigid rather than dynamic."
FT /evidence="ECO:0000269|PubMed:17064365"
FT CONFLICT 98
FT /note="A -> T (in Ref. 2; AAA22397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 35917 MW; F554AAA82AD8853F CRC64;
MFGIGARDLG IDLGTANTLV FVKGKGIVVR EPSVVALQTD TKSIVAVGND AKNMIGRTPG
NVVALRPMKD GVIADYETTA TMMKYYINQA IKNKGMFARK PYVMVCVPSG ITAVEERAVI
DATRQAGARD AYPIEEPFAA AIGANLPVWE PTGSMVVDIG GGTTEVAIIS LGGIVTSQSI
RVAGDEMDDA IINYIRKTYN LMIGDRTAEA IKMEIGSAEA PEESDNMEIR GRDLLTGLPK
TIEITGKEIS NALRDTVSTI VEAVKSTLEK TPPELAADIM DRGIVLTGGG ALLRNLDKVI
SEETKMPVLI AEDPLDCVAI GTGKALEHIH LFKGKTR
