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MetaCyc Enzyme: meso-diaminopimelic acid-D-alanyl endopeptidase / D-alanyl-D-alanine carboxypeptidase

Gene: dacB Accession Numbers: EG10202 (MetaCyc), b3182, ECK3171

Synonyms: D-alanyl-D-alanine carboxypeptidase, fraction B; penicillin-binding protein 4, PBP4

Species: Escherichia coli K-12 substr. MG1655

Summary:
PBP4 is a penicillin-sensitive protein that catalyzes both D-alanyl-D-alanine carboxypeptidase and meso-diaminopimelic acid-D-alanyl endopeptidase activities, though the former has been shown to occur at low levels.

The structures of PBP4 alone and complexed with various antibiotics have been determined by X-ray crystallography to resolutions of 1.55 - 2.8 Å [Thunnissen95, Kishida06]. PBP4 has a twenty-residue amino-terminal signal sequence which is cleaved in mature protein [Mottl91], though it was predicted that this leader sequence is not required for membrane insertion [Davies88]. It also has the characteristic β-lactamase / penicillin-binding protein active site motifs of serine-x-x-lysine, serine-x-asparagine and lysine-threonine-glycine [Mottl91]. Site directed mutagenesis has been used to study the active site of PBP4 [Clarke09]. PBP4 is similar to class A β-lactamases, but contains an extra domain of unkown function between its SxxK and SxN fingerprints [Mottl91, Mottl92]. PBP4 has two disulfide bridges formed by the pairs cysteine-139-cysteine-153 and cysteine-197-cysteine-214 [Mottl92]. The formation of the disulfide bridges is catalyzed by DsbB [Missiakas93]. PBP4 forms an alpha helical structure in the presence of lipid, but unlike PBP5 appears to favor surface rather than deep interaction with membranes [Harris02]. This interaction involves electrostatic rather than hydrophobic forces [Harris98a]. PBP4 can be purified with the dye cibacron navyblue 2G-E [Mottl91a]. PBP4 fractionated with either PBP6 and PBP7; PBP1a, PBP1b, PBP2, PBP3, and PBP5; or PBP1a, PBP1b, PBP1c, PBP2, and PBP3 in membrane vesicles depending on the method used [Leidenix89, Jacoby88].

Purified PBP4 hydrolyzes the D-alanyl-γ-meso-2,6-diaminopimelyl peptide bond of isolated dimeric muropeptides [Korat91].

A dacB mutant lacks D-alanine carboxypeptidase 1B activity [Matsuhashi77, Suzuki78a]. A dacB mutant is defective for transpeptidation of newly inserted murein and for attachment to LppA, but not for transpeptidation during addition of new murein [dePedro81]. A dacA dacB mutant has very little D-alanine carboxypeptidase activity or transpeptidase activity defined as attachment of glycine to the murein tetrapeptide [Matsuhashi78, Matsuhashi79]. Quadruple dacA dacB dacC dacD mutants are viable, as are strains deleted for eight of the known penicillin-binding proteins, PBP4 among them [Baquero96, Denome99]. PBP4 is not required for viability [Vega06]. mepA mepB dacB triple mutants grew normally [Iida83]. Overexpression of dacB results in reduced numbers of murein crosslinks and murein pentapeptides in vitro and in vivo [Korat91]. Overexpression of dacB during early exponential growth leads to cell lysis [Nelson01]. A dacB dacA pbpG, dacB dacA dacD, dacB dacA ftsZ84, or dacB dacA dacC mutant has abnormal cellular morphology [Meberg04, Varma04, Nelson01]. PBP4 is involved in peptidoglycan catabolism during cell division in mutants lacking other peptidoglycan metabolizing enzymes such as AmiC, PBP5, PBP6, and PBP7 [Priyadarshini06]. ftsZ84 dacB pbpG mutants lyse at the nonpermissive temperature [Varma04]. Inhibition of FtsZ by Sula in a dacA dacB mutant results in growth of spiral-shaped cells [Varma04]. An amiA amiB amiC mepA pbpG mutant forms long chains of undivided cells due to a reduced ability to cleave murein septa [Heidrich02]. The amount of PBP4 is decreased in minicells [Obermann94].

Reviews: [Ghosh08, Han06, Scheffers05, Goffin02, Goffin98, Holtje98, Nanninga98, Massova98, Gittins94]

Citations: [Spratt75a, Derouaux08, Meisel03, dePedro03, Nelson02, Meberg01, Vollmer00, Nelson00, Lazar98, Sanders97a, Harris97a, Fusetti96, Engel92a, Begg90, Keck90, Tuomanen87, Kraus87, Kraus85, Curtis81, Spratt80, Tamura80, Amaral86a, Tamaki77, Tamura76]

Locations: periplasmic space, inner membrane

Map Position: [3,326,985 -> 3,328,418]

Molecular Weight of Polypeptide: 51.798 kD (from nucleotide sequence), 49.0 kD (experimental) [Korat91 ]

Unification Links: ASAP:ABE-0010458 , CGSC:885 , EchoBASE:EB0198 , EcoGene:EG10202 , EcoliWiki:b3182 , ModBase:P24228 , OU-Microarray:b3182 , PortEco:dacB , PR:PRO_000022393 , Pride:P24228 , Protein Model Portal:P24228 , RefSeq:NP_417649 , RegulonDB:EG10202 , SMR:P24228 , String:511145.b3182 , UniProt:P24228

Relationship Links: InterPro:IN-FAMILY:IPR000667 , InterPro:IN-FAMILY:IPR012338 , PDB:Structure:2EX2 , PDB:Structure:2EX6 , PDB:Structure:2EX8 , PDB:Structure:2EX9 , PDB:Structure:2EXA , PDB:Structure:2EXB , Pfam:IN-FAMILY:PF02113 , Prints:IN-FAMILY:PR00922

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0000270 - peptidoglycan metabolic process Inferred from experiment [Korat91]
GO:0008360 - regulation of cell shape Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Nelson01, Varma04, Meberg04]
GO:0009253 - peptidoglycan catabolic process Inferred from experiment [Korat91]
GO:0009254 - peptidoglycan turnover Inferred from experiment [Korat91]
GO:0016998 - cell wall macromolecule catabolic process Inferred from experiment [Korat91]
GO:0043093 - FtsZ-dependent cytokinesis Inferred from experiment [Heidrich02]
GO:0071555 - cell wall organization Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Korat91]
GO:0006508 - proteolysis Inferred by computational analysis [GOA01a]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a]
GO:0009252 - peptidoglycan biosynthetic process Inferred by computational analysis [UniProtGOA12, UniProtGOA11a]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11a]
GO:0051301 - cell division Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004175 - endopeptidase activity Inferred from experiment [Korat91]
GO:0004180 - carboxypeptidase activity Inferred from experiment [Matsuhashi77, Suzuki78a]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0008658 - penicillin binding Inferred from experiment [Spratt77a]
GO:0009002 - serine-type D-Ala-D-Ala carboxypeptidase activity Inferred from experiment Inferred by computational analysis [GOA01, Matsuhashi77]
GO:0004185 - serine-type carboxypeptidase activity Inferred by computational analysis [GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment [Matsuhashi77]
GO:0005886 - plasma membrane [Jacoby88]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: cell processes protection drug resistance/sensitivity
cell structure murein
metabolism biosynthesis of macromolecules (cellular constituents) murein (peptidoglycan)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: meso-diaminopimelic acid-D-alanyl endopeptidase

EC Number: 3.4.-.-

peptidoglycan D-alanyl-DAP crosslink[periplasmic space] + H2O[periplasmic space] <=> peptidoglycan tetrapeptide, glycan chain 1[periplasmic space] + peptidoglycan tetrapeptide, glycan chain 2[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Inhibitors (Unknown Mechanism): cephalexin [Eberhardt03]


Sequence Features

Feature Class Location Common Name Citations Comment
Signal-Sequence 1 -> 20 PBP4 signal sequence
[Mottl91]
 
Chain 21 -> 477  
[UniProt09]
UniProt: D-alanyl-D-alanine carboxypeptidase dacB;
Active-Site 62  
[UniProt10]
UniProt: Acyl-ester intermediate;
Active-Site 65  
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Protein-Segment 90 -> 263  
[UniProt10a]
UniProt: Absent in class-A beta-lactamases; Sequence Annotation Type: region of interest;
Sequence-Conflict 261  
[Kishida06, UniProt10]
Alternate sequence: Y; UniProt: (in Ref. 5);
Active-Site 306  
[UniProt10a]
UniProt: Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 417  
[UniProt10a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 427  
[Mottl91, UniProt10]
Alternate sequence: Q; UniProt: (in Ref. 1; CAA42643);

History:
10/20/97 Gene b3182 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10202; confirmed by SwissProt match.


References

Amaral86a: Amaral L, Schwarz U, Lorian V (1986). "Penicillin-binding proteins of filaments of Escherichia coli induced by low concentrations of nalidixic acid, oxolinic acid, novobiocin or nitrofurantoin." Drugs Exp Clin Res 12(8);653-6. PMID: 3530676

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Baquero96: Baquero MR, Bouzon M, Quintela JC, Ayala JA, Moreno F (1996). "dacD, an Escherichia coli gene encoding a novel penicillin-binding protein (PBP6b) with DD-carboxypeptidase activity." J Bacteriol 178(24);7106-11. PMID: 8955390

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

Clarke09: Clarke TB, Kawai F, Park SY, Tame JR, Dowson CG, Roper DI (2009). "Mutational analysis of the substrate specificity of Escherichia coli penicillin binding protein 4." Biochemistry 48(12);2675-83. PMID: 19209901

Curtis81: Curtis SJ, Strominger JL (1981). "Purification of penicillin-binding protein 2 of Escherichia coli." J Bacteriol 145(1);398-403. PMID: 7007320

Davies88: Davies DB, Shohayeb M, Chopra I (1988). "Prediction of signal sequence-dependent protein translocation in bacteria: assessment of the Escherichia coli minicell system." Biochem Biophys Res Commun 150(1);371-5. PMID: 2447893

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

dePedro03: de Pedro MA, Young KD, Holtje JV, Schwarz H (2003). "Branching of Escherichia coli cells arises from multiple sites of inert peptidoglycan." J Bacteriol 185(4);1147-52. PMID: 12562782

dePedro81: de Pedro MA, Schwarz U (1981). "Heterogeneity of newly inserted and preexisting murein in the sacculus of Escherichia coli." Proc Natl Acad Sci U S A 78(9);5856-60. PMID: 7029548

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

Eberhardt03: Eberhardt C, Kuerschner L, Weiss DS (2003). "Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams." J Bacteriol 185(13);3726-34. PMID: 12813065

Engel92a: Engel H, van Leeuwen A, Dijkstra A, Keck W (1992). "Enzymatic preparation of 1,6-anhydro-muropeptides by immobilized murein hydrolases from Escherichia coli fused to staphylococcal protein A." Appl Microbiol Biotechnol 37(6);772-83. PMID: 1369491

Fusetti96: Fusetti F, Dijkstra BW (1996). "Purification and light-scattering analysis of penicillin-binding protein 4 from Escherichia coli." Microb Drug Resist 2(1);73-6. PMID: 9158725

Ghosh08: Ghosh AS, Chowdhury C, Nelson DE (2008). "Physiological functions of D-alanine carboxypeptidases in Escherichia coli." Trends Microbiol 16(7);309-17. PMID: 18539032

Gittins94: Gittins JR, Phoenix DA, Pratt JM (1994). "Multiple mechanisms of membrane anchoring of Escherichia coli penicillin-binding proteins." FEMS Microbiol Rev 13(1);1-12. PMID: 8117464

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Goffin02: Goffin C, Ghuysen JM (2002). "Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent." Microbiol Mol Biol Rev 66(4);702-38, table of contents. PMID: 12456788

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

Han06: Han MJ, Lee SY (2006). "The Escherichia coli proteome: past, present, and future prospects." Microbiol Mol Biol Rev 70(2);362-439. PMID: 16760308

Harris02: Harris F, Brandenburg K, Seydel U, Phoenix D (2002). "Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction." Eur J Biochem 269(23);5821-9. PMID: 12444970

Harris97a: Harris F, Phoenix DA (1997). "An investigation into the ability of C-terminal homologues of Escherichia coli low molecular mass penicillin-binding proteins 4, 5 and 6 to undergo membrane interaction." Biochimie 79(4);171-4. PMID: 9242980

Harris98a: Harris F, Demel R, de Kruijff B, Phoenix DA (1998). "An investigation into the lipid interactions of peptides corresponding to the C-terminal anchoring domains of Escherichia coli penicillin-binding proteins 4, 5 and 6." Biochim Biophys Acta 1415(1);10-22. PMID: 9858668

Heidrich02: Heidrich C, Ursinus A, Berger J, Schwarz H, Holtje JV (2002). "Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli." J Bacteriol 184(22);6093-9. PMID: 12399477

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

Iida83: Iida K, Hirota Y, Schwarz U (1983). "Mutants of Escherichia coli defective in penicillin-insensitive murein DD-endopeptidase." Mol Gen Genet 189(2);215-21. PMID: 6343788

Jacoby88: Jacoby GH, Young KD (1988). "Unequal distribution of penicillin-binding proteins among inner membrane vesicles of Escherichia coli." J Bacteriol 170(8);3660-7. PMID: 3042758

Keck90: Keck W, van Leeuwen AM, Huber M, Goodell EW (1990). "Cloning and characterization of mepA, the structural gene of the penicillin-insensitive murein endopeptidase from Escherichia coli." Mol Microbiol 4(2);209-19. PMID: 2187143

Kishida06: Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR (2006). "Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics." Biochemistry 45(3);783-92. PMID: 16411754

Korat91: Korat B, Mottl H, Keck W (1991). "Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition." Mol Microbiol 5(3);675-84. PMID: 2046551

Kraus85: Kraus W, Glauner B, Holtje JV (1985). "UDP-N-acetylmuramylpentapeptide as acceptor in murein biosynthesis in Escherichia coli membranes and ether-permeabilized cells." J Bacteriol 162(3);1000-4. PMID: 3888951

Kraus87: Kraus W, Holtje JV (1987). "Two distinct transpeptidation reactions during murein synthesis in Escherichia coli." J Bacteriol 169(7);3099-103. PMID: 3298212

Lazar98: Lazar SW, Almiron M, Tormo A, Kolter R (1998). "Role of the Escherichia coli SurA protein in stationary-phase survival." J Bacteriol 180(21);5704-11. PMID: 9791122

Leidenix89: Leidenix MJ, Jacoby GH, Henderson TA, Young KD (1989). "Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatography." J Bacteriol 171(10);5680-6. PMID: 2676988

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

Matsuhashi77: Matsuhashi M, Takagaki Y, Maruyama IN, Tamaki S, Nishimura Y, Suzuki H, Ogino U, Hirota Y (1977). "Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity." Proc Natl Acad Sci U S A 74(7);2976-9. PMID: 331322

Matsuhashi78: Matsuhashi M, Maruyama IN, Takagaki Y, Tamaki S, Nishimura Y, Hirota Y (1978). "Isolation of a mutant of Escherichia coli lacking penicillin-sensitive D-alanine carboxypeptidase IA." Proc Natl Acad Sci U S A 75(6);2631-5. PMID: 351612

Matsuhashi79: Matsuhashi M, Tamaki S, Curtis SJ, Strominger JL (1979). "Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity." J Bacteriol 137(1);644-7. PMID: 368033

Meberg01: Meberg BM, Sailer FC, Nelson DE, Young KD (2001). "Reconstruction of Escherichia coli mrcA (PBP 1a) mutants lacking multiple combinations of penicillin binding proteins." J Bacteriol 183(20);6148-9. PMID: 11567017

Meberg04: Meberg BM, Paulson AL, Priyadarshini R, Young KD (2004). "Endopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coli." J Bacteriol 186(24);8326-36. PMID: 15576782

Meisel03: Meisel U, Holtje JV, Vollmer W (2003). "Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli." J Bacteriol 185(18);5342-8. PMID: 12949085

Missiakas93: Missiakas D, Georgopoulos C, Raina S (1993). "Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo." Proc Natl Acad Sci U S A 90(15);7084-8. PMID: 7688471

Mottl91: Mottl H, Terpstra P, Keck W (1991). "Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins." FEMS Microbiol Lett 62(2-3);213-20. PMID: 2040429

Mottl91a: Mottl H, Keck W (1991). "Purification of penicillin-binding protein 4 of Escherichia coli as a soluble protein by dye-affinity chromatography." Eur J Biochem 200(3);767-73. PMID: 1833192

Mottl92: Mottl H, Nieland P, de Kort G, Wierenga JJ, Keck W (1992). "Deletion of an additional domain located between SXXK and SXN active-site fingerprints in penicillin-binding protein 4 from Escherichia coli." J Bacteriol 174(10);3261-9. PMID: 1577694

Nanninga98: Nanninga N (1998). "Morphogenesis of Escherichia coli." Microbiol Mol Biol Rev 62(1);110-29. PMID: 9529889

Nelson00: Nelson DE, Young KD (2000). "Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli." J Bacteriol 182(6);1714-21. PMID: 10692378

Nelson01: Nelson DE, Young KD (2001). "Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli." J Bacteriol 183(10);3055-64. PMID: 11325933

Nelson02: Nelson DE, Ghosh AS, Paulson AL, Young KD (2002). "Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli." J Bacteriol 184(13);3630-9. PMID: 12057958

Obermann94: Obermann W, Holtje JV (1994). "Alterations of murein structure and of penicillin-binding proteins in minicells from Escherichia coli." Microbiology 140 ( Pt 1);79-87. PMID: 8162193

Priyadarshini06: Priyadarshini R, Popham DL, Young KD (2006). "Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli." J Bacteriol 188(15);5345-55. PMID: 16855223

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Sanders97a: Sanders CC, Bradford PA, Ehrhardt AF, Bush K, Young KD, Henderson TA, Sanders WE (1997). "Penicillin-binding proteins and induction of AmpC beta-lactamase." Antimicrob Agents Chemother 41(9);2013-5. PMID: 9303404

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

Spratt75a: Spratt BG, Pardee AB (1975). "Penicillin-binding proteins and cell shape in E. coli." Nature 254(5500);516-7. PMID: 1091862

Spratt77a: Spratt BG (1977). "Properties of the penicillin-binding proteins of Escherichia coli K12,." Eur J Biochem 72(2);341-52. PMID: 319999

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

Suzuki78a: Suzuki H, Nishimura Y, Hirota Y (1978). "On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins." Proc Natl Acad Sci U S A 75(2);664-8. PMID: 345275

Tamaki77: Tamaki S, Nakajima S, Matsuhashi M (1977). "Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro." Proc Natl Acad Sci U S A 74(12);5472-6. PMID: 341159

Tamura76: Tamura T, Imae Y, Strominger JL (1976). "Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli." J Biol Chem 251(2);414-23. PMID: 1391

Tamura80: Tamura T, Suzuki H, Nishimura Y, Mizoguchi J, Hirota Y (1980). "On the process of cellular division in Escherichia coli: isolation and characterization of penicillin-binding proteins 1a, 1b, and 3." Proc Natl Acad Sci U S A 77(8);4499-503. PMID: 7001458

Thunnissen95: Thunnissen MM, Fusetti F, de Boer B, Dijkstra BW (1995). "Purification, crystallisation and preliminary X-ray analysis of penicillin binding protein 4 from Escherichia coli, a protein related to class A beta-lactamases." J Mol Biol 247(2);149-53. PMID: 7707365

Tuomanen87: Tuomanen E, Schwartz J (1987). "Penicillin-binding protein 7 and its relationship to lysis of nongrowing Escherichia coli." J Bacteriol 169(11);4912-5. PMID: 3312163

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: 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."

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

Varma04: Varma A, Young KD (2004). "FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli." J Bacteriol 186(20);6768-74. PMID: 15466028

Vega06: Vega D, Ayala JA (2006). "The DD-carboxypeptidase activity encoded by pbp4B is not essential for the cell growth of Escherichia coli." Arch Microbiol 185(1):23-7. PMID: 16402224

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


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, biocyc13.