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Escherichia coli K-12 substr. MG1655 Polypeptide: rod shape-determining membrane protein; sensitivity to radiation and drugs



Gene: mrdB Accession Numbers: EG10607 (EcoCyc), b0634, ECK0627

Synonyms: mdrB, rodA

Regulation Summary Diagram: ?

Regulation summary diagram for mrdB

Summary:
mrdB (formerly rodA) encodes an inner membrane protein that is involved in the synthesis of cylindrical peptidoglycan.

mrdB mutants grow as round cells at elevated temperatures and are resistant to the penicillin antibiotic, mecillinan [Matsuzawa73, Iwaya78, Tamaki80, Matsuzawa80]. MrdB is not made as a preprotein; MrdB is not a penicillin binding protein (PBP) [Stoker83].

mrdB and mrdA (encoding a monofunctional transpeptidase, PBP2) are transcribed together - the operon may also include three other genes - rlpA, rlmH and rsfS [Matsuzawa89, MendozaVargas09]. mrdB may also be transcribed independently from a promoter located within mrdA [Asoh83].

MrdB is required for the expression of mrdA encoded peptidoglycan synthetase activity, although the exact nature of it's contribution is not known [Ishino86]. MrdB is predicted to contain 10 transmembrane segments [Holtje98] and has sequence similarity to the lipid II flippase, FtsW [Ikeda89]. MrdB A234T and MrdB T249P mutations suppress the slow growth phenotype and shape defect of ΔrodZ cells [Shiomi13].

mrd: murein D [Tamaki80]

Citations: [Matsuhashi90, Spratt80, Begg85, Begg86, Vinella93, Begg90, Garcia91, Begg98, dePedro01, Bylund91]

Locations: inner membrane

Map Position: [664,424 <- 665,536] (14.32 centisomes, 52°)
Length: 1113 bp / 370 aa

Molecular Weight of Polypeptide: 40.476 kD (from nucleotide sequence), 31 kD (experimental) [Stoker83 ]

Unification Links: ASAP:ABE-0002173 , CGSC:18145 , DIP:DIP-48062N , EchoBASE:EB0602 , EcoGene:EG10607 , EcoliWiki:b0634 , Mint:MINT-1235519 , OU-Microarray:b0634 , PortEco:mrdB , PR:PRO_000023288 , Pride:P0ABG7 , Protein Model Portal:P0ABG7 , RefSeq:NP_415167 , RegulonDB:EG10607 , String:511145.b0634 , UniProt:P0ABG7

Relationship Links: InterPro:IN-FAMILY:IPR001182 , InterPro:IN-FAMILY:IPR011923 , InterPro:IN-FAMILY:IPR018365 , Panther:IN-FAMILY:PTHR30474 , Panther:IN-FAMILY:PTHR30474:SF1 , Pfam:IN-FAMILY:PF01098 , Prosite:IN-FAMILY:PS00428

In Paralogous Gene Group: 587 (2 members)

GO Terms:

Biological Process: GO:0008360 - regulation of cell shape Inferred by computational analysis Inferred from experiment [Spratt80, UniProtGOA11a, GOA01a, Matsuzawa80, Shiomi13]
GO:0009252 - peptidoglycan biosynthetic process Inferred from experiment [Ishino86]
GO:0007049 - cell cycle Inferred by computational analysis [GOA01a]
GO:0051301 - cell division Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Stoker83, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processes cell division
cell structure membrane
transport Putative uncharacterized transport protein

Essentiality data for mrdB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Revised 20-Nov-2014 by Mackie A , Macquarie University


Sequence Features

Protein sequence of rod shape-determining membrane protein; sensitivity to radiation and drugs with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 20 -> 40
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 50 -> 70
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 75 -> 95
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 136 -> 156
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 160 -> 180
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 183 -> 203
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Variant 234
[Shiomi13]
suppressor mutation A→T restores growth and rod shape to cells lacking RodZ
Sequence-Variant 249
[Shiomi13]
suppressor mutation T→P restores growth and rod shape to cells lacking RodZ
Transmembrane-Region 263 -> 283
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 312 -> 332
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 336 -> 356
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram

Notes:

History:
10/20/97 Gene b0634 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10607; confirmed by SwissProt match.


References

Asoh83: Asoh S, Matsuzawa H, Matsuhashi M, Ohta T (1983). "Molecular cloning and characterization of the genes (pbpA and rodA) responsible for the rod shape of Escherichia coli K-12: analysis of gene expression with transposon Tn5 mutagenesis and protein synthesis directed by constructed plasmids." J Bacteriol 154(1);10-6. PMID: 6300030

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Begg85: Begg KJ, Donachie WD (1985). "Cell shape and division in Escherichia coli: experiments with shape and division mutants." J Bacteriol 163(2);615-22. PMID: 3894330

Begg86: Begg KJ, Spratt BG, Donachie WD (1986). "Interaction between membrane proteins PBP3 and rodA is required for normal cell shape and division in Escherichia coli." J Bacteriol 167(3);1004-8. PMID: 3017915

Begg90: Begg KJ, Takasuga A, Edwards DH, Dewar SJ, Spratt BG, Adachi H, Ohta T, Matsuzawa H, Donachie WD (1990). "The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide." J Bacteriol 172(12);6697-703. PMID: 2254246

Begg98: Begg KJ, Donachie WD (1998). "Division planes alternate in spherical cells of Escherichia coli." J Bacteriol 180(9);2564-7. PMID: 9573213

Bylund91: Bylund JE, Haines MA, Walsh K, Bouloc P, D'Ari R, Higgins ML (1991). "Buoyant density studies of several mecillinam-resistant and division mutants of Escherichia coli." J Bacteriol 173(17);5396-402. PMID: 1885519

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

dePedro01: de Pedro MA, Donachie WD, Holtje JV, Schwarz H (2001). "Constitutive septal murein synthesis in Escherichia coli with impaired activity of the morphogenetic proteins RodA and penicillin-binding protein 2." J Bacteriol 183(14);4115-26. PMID: 11418550

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Garcia91: Garcia del Portillo F, de Pedro MA (1991). "Penicillin-binding protein 2 is essential for the integrity of growing cells of Escherichia coli ponB strains." J Bacteriol 173(14);4530-2. PMID: 2066344

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Holtje98: Holtje JV (1998). "Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli." Microbiol Mol Biol Rev 62(1);181-203. PMID: 9529891

Ikeda89: Ikeda M, Sato T, Wachi M, Jung HK, Ishino F, Kobayashi Y, Matsuhashi M (1989). "Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively." J Bacteriol 171(11);6375-8. PMID: 2509435

Ishino86: Ishino F, Park W, Tomioka S, Tamaki S, Takase I, Kunugita K, Matsuzawa H, Asoh S, Ohta T, Spratt BG (1986). "Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein." J Biol Chem 261(15);7024-31. PMID: 3009484

Iwaya78: Iwaya M, Jones CW, Khorana J, Strominger JL (1978). "Mapping of the mecillinam-resistant, round morphological mutants of Escherichia coli." J Bacteriol 133(1);196-202. PMID: 201607

Matsuhashi90: Matsuhashi M, Wachi M, Ishino F (1990). "Machinery for cell growth and division: penicillin-binding proteins and other proteins." Res Microbiol 141(1);89-103. PMID: 2114032

Matsuzawa73: Matsuzawa H, Hayakawa K, Sato T, Imahori K (1973). "Characterization and genetic analysis of a mutant of Escherichia coli K-12 with rounded morphology." J Bacteriol 115(1);436-42. PMID: 4577747

Matsuzawa80: Matsuzawa H, Asoh S, Ohta S, Tamaki S, Matsuhashi M (1980). "Further studies on rodA mutant: a round morphological mutant of Escherichia coli K-12 with wild-type penicillin-binding protein 2." Agricultural and Biological Chemistry 44:2937-2941.

Matsuzawa89: Matsuzawa H, Asoh S, Kunai K, Muraiso K, Takasuga A, Ohta T (1989). "Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon." J Bacteriol 171(1);558-60. PMID: 2644207

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

Shiomi13: Shiomi D, Toyoda A, Aizu T, Ejima F, Fujiyama A, Shini T, Kohara Y, Niki H (2013). "Mutations in cell elongation genes mreB, mrdA and mrdB suppress the shape defect of RodZ-deficient cells." Mol Microbiol 87(5);1029-44. PMID: 23301723

Spratt80: Spratt BG, Boyd A, Stoker N (1980). "Defective and plaque-forming lambda transducing bacteriophage carrying penicillin-binding protein-cell shape genes: genetic and physical mapping and identification of gene products from the lip-dacA-rodA-pbpA-leuS region of the Escherichia coli chromosome." J Bacteriol 143(2);569-81. PMID: 6451612

Stoker83: Stoker NG, Pratt JM, Spratt BG (1983). "Identification of the rodA gene product of Escherichia coli." J Bacteriol 155(2);854-9. PMID: 6348029

Tamaki80: Tamaki S, Matsuzawa H, Matsuhashi M (1980). "Cluster of mrdA and mrdB genes responsible for the rod shape and mecillinam sensitivity of Escherichia coli." J Bacteriol 141(1);52-7. PMID: 6243629

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Vinella93: Vinella D, Joseleau-Petit D, Thevenet D, Bouloc P, D'Ari R (1993). "Penicillin-binding protein 2 inactivation in Escherichia coli results in cell division inhibition, which is relieved by FtsZ overexpression." J Bacteriol 175(20);6704-10. PMID: 8407846


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Sat Apr 25, 2015, biocyc12.