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ECOLI:MREB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) mreB (synonyms: envB, rodY)
Protein Name(s) Rod shape-determining protein MreB
External Links
UniProt P0A9X4
EMBL M22055
U18997
U00096
AP009048
M31792
RefSeq NP_417717.2
YP_491434.1
ProteinModelPortal P0A9X4
SMR P0A9X4
DIP DIP-31874N
IntAct P0A9X4
MINT MINT-1222190
STRING 511145.b3251
TCDB 9.B.157.1.3
PaxDb P0A9X4
PRIDE P0A9X4
EnsemblBacteria AAC76283
BAE77293
GeneID 12932946
948588
KEGG ecj:Y75_p3170
eco:b3251
PATRIC 32121928
EchoBASE EB0603
EcoGene EG10608
eggNOG COG1077
HOGENOM HOG000019757
InParanoid P0A9X4
KO K03569
OMA GIVCDKS
OrthoDB EOG66QM00
PhylomeDB P0A9X4
BioCyc EcoCyc:EG10608-MONOMER
ECOL316407:JW3220-MONOMER
PRO PR:P0A9X4
Proteomes UP000000318
UP000000625
Genevestigator P0A9X4
GO GO:0005856
GO:0042802
GO:0000902
GO:0051782
GO:0008360
GO:0051983
InterPro IPR004753
Pfam PF06723
PRINTS PR01652
TIGRFAMs TIGR00904

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005200

cytoskeleton

PMID:20439764[1]

ECO:0000314

C

Fig. 2. The force-displacement curves and bending stiffness of single E. coli cells., Fig. 3. Statistics on the A22-induced decrease in flexural rigidity.

complete

GO:0000902

cell morphogenesis

PMID:20439764[1]

ECO:0000314

P

Fig. 2. The force-displacement curves and bending stiffness of single E. coli cells., Fig. 3. Statistics on the A22-induced decrease in flexural rigidity.

complete

GO:0009408

response to heat

PMID:2822655[2]

ECO:0000315

P

Table 2. Cell shapes and sensitivities of mre mutants to P-lactam antibiotics by temperature.

complete

GO:0005856

cytoskeleton

PMID:11544518[3]

ECO:0000250

pdb:1ATN


C

Figure 3. Structural similarity of MreB to actin.

complete

GO:0005200

structural constituent of cytoskeleton

PMID:19346310[4]

ECO:0000270

F

Fig 2

complete
CACAO 3675

GO:0043164

Gram-negative-bacterium-type cell wall biogenesis

PMID:19346310[4]

ECO:0000316

UniProtKB:P0A9A6


P

Table 1 Strain 2 MreB can tether peptidoglycan synthesis via a PBP2 pathway independently of FtsZ, producing a rod-shaped cell

complete
CACAO 3943

GO:0051782

negative regulation of cell division

PMID:2656641[5]

ECO:0000315

P

Figure 4A. shows filamentous cell growth in strains carrying additional copies of mreB gene, a result of inhibition of cell division.

Table 1. shows overproduction of cell division gene ftsI in mreB mutant cells.

complete
CACAO 5363

involved_in

GO:0051782

negative regulation of cell division

PMID:2656641[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23756461[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9X4

F

occurs_in:(GO:0030428)

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22515815[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9X4

F

occurs_in:(GO:0030428)

Seeded From UniProt

complete

involved_in

GO:0051983

regulation of chromosome segregation

PMID:19187760[8]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:mreC
EcoliWiki:mreD

P

Seeded From UniProt

complete

involved_in

GO:0051983

regulation of chromosome segregation

PMID:14517265[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043093

FtsZ-dependent cytokinesis

PMID:23756461[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043093

FtsZ-dependent cytokinesis

PMID:23756461[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15612918[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0031226

intrinsic component of plasma membrane

PMID:21816350[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:17993535[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

PMID:15612918[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:15612918[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

PMID:19220747[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

PMID:14517265[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

PMID:12766229[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000902

cell morphogenesis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004753

P

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0133

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Wang, S et al. (2010) Actin-like cytoskeleton filaments contribute to cell mechanics in bacteria. Proc. Natl. Acad. Sci. U.S.A. 107 9182-5 PubMed GONUTS page
  2. ↑ Wachi, M et al. (1987) Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J. Bacteriol. 169 4935-40 PubMed GONUTS page
  3. ↑ van den Ent, F et al. (2001) Prokaryotic origin of the actin cytoskeleton. Nature 413 39-44 PubMed GONUTS page
  4. ↑ 4.0 4.1 Varma, A & Young, KD (2009) In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2. J. Bacteriol. 191 3526-33 PubMed GONUTS page
  5. ↑ 5.0 5.1 Wachi, M & Matsuhashi, M (1989) Negative control of cell division by mreB, a gene that functions in determining the rod shape of Escherichia coli cells. J. Bacteriol. 171 3123-7 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 Fenton, AK & Gerdes, K (2013) Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli. EMBO J. 32 1953-65 PubMed GONUTS page
  7. ↑ Masuda, H et al. (2012) YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli. Mol. Microbiol. 84 979-89 PubMed GONUTS page
  8. ↑ Madabhushi, R & Marians, KJ (2009) Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli. Mol. Cell 33 171-80 PubMed GONUTS page
  9. ↑ 9.0 9.1 Kruse, T et al. (2003) Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J. 22 5283-92 PubMed GONUTS page
  10. ↑ 10.0 10.1 10.2 Kruse, T et al. (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol. Microbiol. 55 78-89 PubMed GONUTS page
  11. ↑ Salje, J et al. (2011) Direct membrane binding by bacterial actin MreB. Mol. Cell 43 478-87 PubMed GONUTS page
  12. ↑ Bendezú, FO & de Boer, PA (2008) Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J. Bacteriol. 190 1792-811 PubMed GONUTS page
  13. ↑ Vats, P et al. (2009) Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Mol. Microbiol. 72 170-82 PubMed GONUTS page
  14. ↑ Shih, YL et al. (2003) Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. U.S.A. 100 7865-70 PubMed GONUTS page
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