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Escherichia coli K-12 substr. MG1655 Enzyme: peptidoglycan glycosyltransferase



Gene: pbpC Accession Numbers: G7322 (EcoCyc), b2519, ECK2515

Synonyms: yfgN, PBP1C

Regulation Summary Diagram: ?

Summary:
PBP1C is one of several HMW penicillin binding proteins (PBPs) of E. coli which catalyse the transglycosylation and transpeptidation of peptidoglycan (murein) precursors in the formation of the murein sacculus. PBP1C (like PBP1A and PBP1B) contains characteristic transglycosylase and transpeptidase amino acid motifs but only transglycosylation activity has been biochemically assayed [Schiffer99]. Additionally, PBP1C does not bind most of the B-lactams known to bind other PBPs leading to the suggestion that PBP1C does not have transpeptidase activity (the transpeptidase region is also responsible for penicillin binding) [Schiffer99].

PBP1C is responsible for 75% of transglycosylase activity in ether pemeabilized cells, but only less than 3% in crude membranes [Schiffer99]. Maximum binding of penicillin to PBP1C occurred at pH 5 [Amaral86a]. PBP1C bound moxalactam poorly [Labia85]. PBP1C does not bind ampicillin or benzylpenicillin derivatives well [Vollmer00], though it has been identified after binding 125I-labeled ampicillin [Wientjes83]. PBP1C has been said to bind furazlocillin [Botta81a].

Deletion of the pbpC gene does not cause an obvious phenotype except for an increase in TetraPenta dimeric muropeptides [Schiffer99]. Overproduction of the PBP1C protein does not rescue the defect of a ponAts ponB double mutant [Schiffer99].

PBP1C interacts with PBP1B, PBP3, PBP4, PBP2 through an unknown periplasmic factor, and MltA [Schiffer99, Vollmer99a]. PBP1C was also found to interact with Slt70 and MltB [vonRechenberg96].

There was no apparent fluctuation in pbpC expression at different points of the cell cycle [Wientjes83].

YfhM homologs in bacteria are often found tightly linked to pbpC leading to the suggestion that they may act together as a defense and repair mechanism to protect the cell from host defenses during colonization [Budd04].

Reviews: [Scheffers05, Goffin98, Holtje98]

Citations: [Derouaux08, Serres05, Denome99, Massova98]

Locations: inner membrane

Map Position: [2,643,035 <- 2,645,347] (56.97 centisomes)
Length: 2313 bp / 770 aa

Molecular Weight of Polypeptide: 85.067 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0008294 , DIP:DIP-10442N , EchoBASE:EB3962 , EcoGene:EG14210 , EcoliWiki:b2519 , Mint:MINT-1308552 , ModBase:P76577 , OU-Microarray:b2519 , PortEco:pbpC , PR:PRO_000023496 , Pride:P76577 , Protein Model Portal:P76577 , RefSeq:NP_417014 , RegulonDB:G7322 , SMR:P76577 , String:511145.b2519 , UniProt:P76577

Relationship Links: CAZy:IN-FAMILY:GT51 , InterPro:IN-FAMILY:IPR001264 , InterPro:IN-FAMILY:IPR001460 , InterPro:IN-FAMILY:IPR009647 , InterPro:IN-FAMILY:IPR011815 , InterPro:IN-FAMILY:IPR012338 , InterPro:IN-FAMILY:IPR023346 , Pfam:IN-FAMILY:PF00905 , Pfam:IN-FAMILY:PF00912 , Pfam:IN-FAMILY:PF06832

In Paralogous Gene Group: 50 (4 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009252 - peptidoglycan biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA01, Schiffer99]
GO:0051781 - positive regulation of cell division Inferred from experiment [Spratt75]
GO:0008360 - regulation of cell shape Inferred by computational analysis [UniProtGOA11]
GO:0071555 - cell wall organization Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0008144 - drug binding Inferred from experiment [Schiffer99, Wientjes83]
GO:0008955 - peptidoglycan glycosyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01, Schiffer99]
GO:0008658 - penicillin binding Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016757 - transferase activity, transferring glycosyl groups Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Barbas86]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, Schiffer99]

MultiFun Terms: cell structure murein
metabolism biosynthesis of macromolecules (cellular constituents) murein (peptidoglycan)

Essentiality data for pbpC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 13-Nov-2008 by Johnson A , JCVI


Enzymatic reaction of: peptidoglycan glycosyltransferase

EC Number: 2.4.1.129

2 ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-γ-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine[periplasmic space] <=> a peptidoglycan dimer (meso-diaminopimelate containing)[periplasmic space] + di-trans,octa-cis-undecaprenyl diphosphate[periplasmic space] + H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: peptidoglycan biosynthesis I (meso-diaminopimelate containing)

Inhibitors (Unknown Mechanism): moenomycin [Schiffer99]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 9 -> 29
[UniProt10]
UniProt: Helical; Signal-anchor for type II membrane protein;; Non-Experimental Qualifier: potential;
Protein-Segment 43 -> 213
[UniProt10]
UniProt: Transglycosylase; Sequence Annotation Type: region of interest;
Protein-Segment 278 -> 559
[UniProt10]
UniProt: Transpeptidase; Sequence Annotation Type: region of interest;
Active-Site 342
[UniProt10]
UniProt: Acyl-ester intermediate; for transpeptidase activity; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Amaral86a: Amaral L, Lee Y, Schwarz U, Lorian V (1986). "Penicillin-binding site on the Escherichia coli cell envelope." J Bacteriol 167(2);492-5. PMID: 3090016

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

Barbas86: Barbas JA, Diaz J, Rodriguez-Tebar A, Vazquez D (1986). "Specific location of penicillin-binding proteins within the cell envelope of Escherichia coli." J Bacteriol 165(1);269-75. PMID: 3510188

Botta81a: Botta GA, Park JT (1981). "Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation." J Bacteriol 145(1);333-40. PMID: 6450748

Budd04: Budd A, Blandin S, Levashina EA, Gibson TJ (2004). "Bacterial alpha2-macroglobulins: colonization factors acquired by horizontal gene transfer from the metazoan genome?." Genome Biol 5(6);R38. PMID: 15186489

Denome99: Denome SA, Elf PK, Henderson TA, Nelson DE, Young KD (1999). "Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis." J Bacteriol 181(13);3981-93. PMID: 10383966

Derouaux08: Derouaux A, Wolf B, Fraipont C, Breukink E, Nguyen-Disteche M, Terrak M (2008). "The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN." J Bacteriol 190(5);1831-4. PMID: 18165305

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

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Goffin98: Goffin C, Ghuysen JM (1998). "Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs." Microbiol Mol Biol Rev 62(4);1079-93. PMID: 9841666

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

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Labia85: Labia R, Baron P, Masson JM (1985). "Binding of latamoxef (moxalactam) and its decarboxylated derivative to Escherichia coli and Pseudomonas aeruginosa penicillin-binding proteins." J Antimicrob Chemother 15(1);9-15. PMID: 3918982

Massova98: Massova I, Mobashery S (1998). "Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases." Antimicrob Agents Chemother 42(1);1-17. PMID: 9449253

Scheffers05: Scheffers DJ, Pinho MG (2005). "Bacterial cell wall synthesis: new insights from localization studies." Microbiol Mol Biol Rev 69(4);585-607. PMID: 16339737

Schiffer99: Schiffer G, Holtje JV (1999). "Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli." J Biol Chem 274(45);32031-9. PMID: 10542235

Serres05: Serres MH, Riley M (2005). "Gene fusions and gene duplications: relevance to genomic annotation and functional analysis." BMC Genomics 6(1);33. PMID: 15757509

Spratt75: Spratt BG (1975). "Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12." Proc Natl Acad Sci U S A 72(8);2999-3003. PMID: 1103132

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 manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Vollmer00: Vollmer W, Holtje JV (2000). "A simple screen for murein transglycosylase inhibitors." Antimicrob Agents Chemother 44(5);1181-5. PMID: 10770749

Vollmer99a: Vollmer W, von Rechenberg M, Holtje JV (1999). "Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli." J Biol Chem 274(10);6726-34. PMID: 10037771

vonRechenberg96: von Rechenberg M, Ursinus A, Holtje JV (1996). "Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis." Microb Drug Resist 2(1);155-7. PMID: 9158739

Wientjes83: Wientjes FB, Olijhoek TJ, Schwarz U, Nanninga N (1983). "Labeling pattern of major penicillin-binding proteins of Escherichia coli during the division cycle." J Bacteriol 153(3);1287-93. PMID: 6337993

Other References Related to Gene Regulation

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


Report Errors or Provide Feedback
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 18.5 on Fri Nov 21, 2014, BIOCYC13B.