MREB_ECOLI
ID MREB_ECOLI Reviewed; 347 AA.
AC P0A9X4; P13519; P76678; Q2M8W3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000255|HAMAP-Rule:MF_02207, ECO:0000305};
DE AltName: Full=Actin-like MreB protein {ECO:0000305};
DE AltName: Full=Rod shape-determining protein MreB {ECO:0000305};
GN Name=mreB {ECO:0000303|PubMed:3049542}; Synonyms=envB, rodY;
GN OrderedLocusNames=b3251, JW3220;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12;
RX PubMed=3049542; DOI=10.1128/jb.170.10.4619-4624.1988;
RA Doi M., Wachi M., Ishino F., Tomioka S., Ito M., Sakagami Y., Suzuki A.,
RA Matsuhashi M.;
RT "Determinations of the DNA sequence of the mreB gene and of the gene
RT products of the mre region that function in formation of the rod shape of
RT Escherichia coli cells.";
RL J. Bacteriol. 170:4619-4624(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-347.
RC STRAIN=K12;
RX PubMed=2687239; DOI=10.1128/jb.171.12.6511-6516.1989;
RA Wachi M., Doi M., Okada Y., Matsuhashi M.;
RT "New mre genes mreC and mreD, responsible for formation of the rod shape of
RT Escherichia coli cells.";
RL J. Bacteriol. 171:6511-6516(1989).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15612918; DOI=10.1111/j.1365-2958.2004.04367.x;
RA Kruse T., Bork-Jensen J., Gerdes K.;
RT "The morphogenetic MreBCD proteins of Escherichia coli form an essential
RT membrane-bound complex.";
RL Mol. Microbiol. 55:78-89(2005).
RN [7]
RP ACTIVITY REGULATION, AND INTERACTION WITH FTSZ AND CBTA.
RC STRAIN=K12 / BW25113;
RX PubMed=21166897; DOI=10.1111/j.1365-2958.2010.07433.x;
RA Tan Q., Awano N., Inouye M.;
RT "YeeV is an Escherichia coli toxin that inhibits cell division by targeting
RT the cytoskeleton proteins, FtsZ and MreB.";
RL Mol. Microbiol. 79:109-118(2011).
RN [8]
RP FUNCTION.
RX PubMed=21903929; DOI=10.1073/pnas.1108999108;
RA van Teeffelen S., Wang S., Furchtgott L., Huang K.C., Wingreen N.S.,
RA Shaevitz J.W., Gitai Z.;
RT "The bacterial actin MreB rotates, and rotation depends on cell-wall
RT assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15822-15827(2011).
RN [9]
RP ACTIVITY REGULATION, AND INTERACTION WITH CPTA.
RC STRAIN=B / BL21-DE3, and K12 / BW25113;
RX PubMed=22239607; DOI=10.1111/j.1574-6968.2012.02496.x;
RA Masuda H., Tan Q., Awano N., Yamaguchi Y., Inouye M.;
RT "A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits
RT polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia
RT coli.";
RL FEMS Microbiol. Lett. 328:174-181(2012).
RN [10]
RP ACTIVITY REGULATION, AND INTERACTION WITH CBEA.
RC STRAIN=K12 / BW25113;
RX PubMed=22515815; DOI=10.1111/j.1365-2958.2012.08068.x;
RA Masuda H., Tan Q., Awano N., Wu K.P., Inouye M.;
RT "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ,
RT antagonizing the CbtA (YeeV) toxicity in Escherichia coli.";
RL Mol. Microbiol. 84:979-989(2012).
RN [11]
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=23235161; DOI=10.1074/jbc.m112.413708;
RA Nurse P., Marians K.J.;
RT "Purification and characterization of Escherichia coli MreB protein.";
RL J. Biol. Chem. 288:3469-3475(2013).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24550515; DOI=10.1073/pnas.1317174111;
RA Ursell T.S., Nguyen J., Monds R.D., Colavin A., Billings G., Ouzounov N.,
RA Gitai Z., Shaevitz J.W., Huang K.C.;
RT "Rod-like bacterial shape is maintained by feedback between cell curvature
RT and cytoskeletal localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E1025-E1034(2014).
CC -!- FUNCTION: Forms membrane-associated dynamic filaments that are
CC essential for cell shape determination (PubMed:15612918,
CC PubMed:21903929). Acts by regulating cell wall synthesis and cell
CC elongation, and thus cell shape (PubMed:21903929). A feedback loop
CC between cell geometry and MreB localization maintains elongated cell
CC shape by targeting cell wall growth to regions of negative cell wall
CC curvature (PubMed:24550515). Filaments rotate around the cell
CC circumference in concert with the cell wall synthesis enzymes. The
CC process is driven by the cell wall synthesis machinery and does not
CC depend on MreB polymerization (PubMed:21903929). Rotation may
CC contribute to the robust maintenance of rod shape (PubMed:21903929).
CC {ECO:0000269|PubMed:15612918, ECO:0000269|PubMed:21903929,
CC ECO:0000269|PubMed:24550515}.
CC -!- ACTIVITY REGULATION: Requires ATP hydrolysis for polymerization
CC (PubMed:23235161). Polymerization is inhibited by toxins CbtA and CptA,
CC as well as by A22 ([S-(3,4-dichlorobenzyl)isothiourea)] all of which
CC cause cell rounding and eventual death. Inhibition by toxin CbtA is
CC neutralized by cytoskeleton bundling-enhancing protein CbeA, inhibition
CC by toxin CptA is neutralized by antitoxin CptB, while inhibition by A22
CC can be neutralized by overexpression of CbeA (PubMed:21166897,
CC PubMed:22239607, PubMed:22515815). {ECO:0000269|PubMed:21166897,
CC ECO:0000269|PubMed:22239607, ECO:0000269|PubMed:22515815,
CC ECO:0000269|PubMed:23235161}.
CC -!- SUBUNIT: Forms polymers in the presence of ATP or GTP
CC (PubMed:23235161). Forms an essential membrane-bound complex with MreC
CC and MreD. Interacts directly with MreC but not with MreD
CC (PubMed:15612918). Interacts with FtsZ, toxins CbtA and CptA, and
CC cytoskeleton bundling-enhancing protein CbeA (PubMed:21166897,
CC PubMed:22239607, PubMed:22515815). {ECO:0000269|PubMed:15612918,
CC ECO:0000269|PubMed:21166897, ECO:0000269|PubMed:22239607,
CC ECO:0000269|PubMed:22515815, ECO:0000269|PubMed:23235161}.
CC -!- INTERACTION:
CC P0A9X4; P76364: cbeA; NbExp=2; IntAct=EBI-371008, EBI-1126877;
CC P0A9X4; P0ABH0: ftsA; NbExp=3; IntAct=EBI-371008, EBI-550562;
CC P0A9X4; P0A9A6: ftsZ; NbExp=7; IntAct=EBI-371008, EBI-370963;
CC P0A9X4; P0A9X4: mreB; NbExp=3; IntAct=EBI-371008, EBI-371008;
CC P0A9X4; P27434: rodZ; NbExp=3; IntAct=EBI-371008, EBI-1129185;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15612918}.
CC Note=Membrane-associated (PubMed:15612918). Preferentially localizes to
CC regions of negative curvature (PubMed:24550515). May associate with the
CC membrane via MreC (PubMed:15612918). Localization depends on MreC, MreD
CC and RodA (PubMed:15612918). {ECO:0000269|PubMed:15612918,
CC ECO:0000269|PubMed:24550515}.
CC -!- DISRUPTION PHENOTYPE: Depletion results in enlarged, spherical cells.
CC {ECO:0000269|PubMed:15612918}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02207, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58054.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M22055; AAA83891.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58054.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76283.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77293.1; -; Genomic_DNA.
DR EMBL; M31792; AAA24154.1; -; Genomic_DNA.
DR RefSeq; NP_417717.2; NC_000913.3.
DR RefSeq; WP_000913396.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P0A9X4; -.
DR SMR; P0A9X4; -.
DR BioGRID; 4261940; 383.
DR ComplexPortal; CPX-5718; Elongasome complex.
DR DIP; DIP-31874N; -.
DR IntAct; P0A9X4; 82.
DR MINT; P0A9X4; -.
DR STRING; 511145.b3251; -.
DR TCDB; 9.B.157.1.3; the cell shape-determining mrebcd (mrebcd) family.
DR jPOST; P0A9X4; -.
DR PaxDb; P0A9X4; -.
DR PRIDE; P0A9X4; -.
DR EnsemblBacteria; AAC76283; AAC76283; b3251.
DR EnsemblBacteria; BAE77293; BAE77293; BAE77293.
DR GeneID; 64728064; -.
DR GeneID; 67517865; -.
DR GeneID; 948588; -.
DR KEGG; ecj:JW3220; -.
DR KEGG; eco:b3251; -.
DR PATRIC; fig|511145.12.peg.3348; -.
DR EchoBASE; EB0603; -.
DR eggNOG; COG1077; Bacteria.
DR HOGENOM; CLU_052037_0_0_6; -.
DR InParanoid; P0A9X4; -.
DR OMA; MVICIPS; -.
DR PhylomeDB; P0A9X4; -.
DR BioCyc; EcoCyc:EG10608-MON; -.
DR PRO; PR:P0A9X4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IDA:EcoCyc.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0099513; C:polymeric cytoskeletal fiber; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IDA:EcoCyc.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:CACAO.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IC:ComplexPortal.
DR GO; GO:0008360; P:regulation of cell shape; IMP:EcoCyc.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP:EcoliWiki.
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; Direct protein sequencing;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..347
FT /note="Cell shape-determining protein MreB"
FT /id="PRO_0000062759"
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 168..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 216..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT BINDING 296..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207"
FT CONFLICT 60..61
FT /note="KQ -> NE (in Ref. 1; AAA83891)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="T -> I (in Ref. 1; AAA83891)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..278
FT /note="QC -> HT (in Ref. 1; AAA83891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 36952 MW; 1393696D8CDAEF93 CRC64;
MLKKFRGMFS NDLSIDLGTA NTLIYVKGQG IVLNEPSVVA IRQDRAGSPK SVAAVGHDAK
QMLGRTPGNI AAIRPMKDGV IADFFVTEKM LQHFIKQVHS NSFMRPSPRV LVCVPVGATQ
VERRAIRESA QGAGAREVFL IEEPMAAAIG AGLPVSEATG SMVVDIGGGT TEVAVISLNG
VVYSSSVRIG GDRFDEAIIN YVRRNYGSLI GEATAERIKH EIGSAYPGDE VREIEVRGRN
LAEGVPRGFT LNSNEILEAL QEPLTGIVSA VMVALEQCPP ELASDISERG MVLTGGGALL
RNLDRLLMEE TGIPVVVAED PLTCVARGGG KALEMIDMHG GDLFSEE
