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Escherichia coli K-12 substr. MG1655 Polypeptide: murein tripeptide ABC transporter / peptide ABC transporter - putative membrane subunit



Gene: oppC Accession Numbers: EG10676 (EcoCyc), b1245, ECK1239

Regulation Summary Diagram: ?

Component of:
murein tripeptide ABC transporter OppBCDFMppA (extended summary available)
peptide ABC transporter OppABCDF (extended summary available)

Summary:
OppC is an integral membrane component of the oligopeptide ABC transporter and the murein tripeptide ABC transporter.

Gene Citations: [Andrews86, Hiles87]

Locations: inner membrane

Map Position: [1,301,858 -> 1,302,766] (28.06 centisomes)
Length: 909 bp / 302 aa

Molecular Weight of Polypeptide: 33.022 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0004176 , CGSC:18088 , EchoBASE:EB0670 , EcoGene:EG10676 , EcoliWiki:b1245 , OU-Microarray:b1245 , PortEco:oppC , PR:PRO_000023463 , Protein Model Portal:P0AFH6 , RefSeq:NP_415761 , RegulonDB:EG10676 , String:511145.b1245 , UniProt:P0AFH6

Relationship Links: InterPro:IN-FAMILY:IPR000515 , InterPro:IN-FAMILY:IPR025966 , Pfam:IN-FAMILY:PF00528 , Pfam:IN-FAMILY:PF12911 , Prosite:IN-FAMILY:PS50928

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11]
GO:0015833 - peptide transport Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]
GO:0043190 - ATP-binding cassette (ABC) transporter complex

MultiFun Terms: cell structure membrane
cell structure murein
metabolism central intermediary metabolism murein turnover, recycling
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, membrane component

Essentiality data for oppC knockouts: ?

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

Subunit of: murein tripeptide ABC transporter OppBCDFMppA

Subunit composition of murein tripeptide ABC transporter OppBCDFMppA = [OppB][OppC][OppD][OppF][MppA]
         murein tripeptide ABC transporter / peptide ABC transporter - putative membrane subunit = OppB (summary available)
         murein tripeptide ABC transporter / peptide ABC transporter - putative membrane subunit = OppC (summary available)
         murein tripeptide ABC transporter / peptide ABC transporter - putative ATP binding subunit = OppD (summary available)
         murein tripeptide ABC transporter / peptide ABC transporter - putative ATP binding subunit = OppF (summary available)
         murein tripeptide ABC transporter OppBCDFMppA - periplasmic binding protein = MppA (summary available)

Summary:
OppABCDF is an ATP-dependent oligopeptide transporter that is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Pearce92]. Based on sequence similarity, OppB and OppC are the membrane components of the ABC transporter, and OppD and OppF are the ATP-binding components of the ABC transporter [Angelopoulos96, Pearce92]. OppA is the periplasmic substrate-binding component, however MppA can replace OppA as a periplasmic-binding component of the transporter when it binds murein tripeptides [Park98].

Binding affinity and competition assays have shown that OppABCDF will transport oligopeptides up to five amino acids in length, but has no affinity for free amino acids [Guyer86, Angelopoulos96]. The system has been observed to function in oligopeptide uptake, as well as recycling of cell wall peptides [Goodell87, Hiles87]. MppA was shown to be required for murein tripeptide transport in a diaminopimelic acid-requiring strain [Park98]. OppD has been purified and identified by direct assays as an ATP-binding component of the OppABCDF oligopeptide transporter [Higgins85]. Insertional mutants of each of the opp genes were constructed, and the opp-minus strains were unable to utilize the peptide Pro-Gly-Gly, normally transported by the wild-type transporter [Hiles87].

When an outer membrane heme receptor is expressed in E. coli, the murein tripeptide ABC transporter is also capable of transporting heme and the heme precursor, δ aminolevulinic acid, from the periplasm into the cytoplasm [Letoffe06]. Binding of heme to purified MppA has been demonstrated and is inhibited by Pro-Phe-Lys [Letoffe06].

Expression of oppABCD increased after long-term adaptation to growth in complex medium with acetate or propionate [Polen03]. Expression of mppA decreased after long-term adaptation to growth in complex medium with acetate or propionate [Polen03]. Expression of mppA was shown to be activated by cyclic AMP receptor protein [Zheng04].

Citations: [Bina03, Li99e, Park93, Lenny80]

Credits:
Created 21-Jun-2006 by Johnson A , TIGR


Enzymatic reaction of: Transport of L-Ala-D-Glu-meso-A2pm (murein tripeptide ABC transporter OppBCDFMppA)


Subunit of: peptide ABC transporter OppABCDF

Subunit composition of peptide ABC transporter OppABCDF = [OppC][OppD][OppF][OppB][OppA]
         murein tripeptide ABC transporter / peptide ABC transporter - putative membrane subunit = OppC (summary available)
         murein tripeptide ABC transporter / peptide ABC transporter - putative ATP binding subunit = OppD (summary available)
         murein tripeptide ABC transporter / peptide ABC transporter - putative ATP binding subunit = OppF (summary available)
         murein tripeptide ABC transporter / peptide ABC transporter - putative membrane subunit = OppB (summary available)
         peptide ABC transporter - periplasmic binding protein = OppA (summary available)

Summary:
OppABCDF is an ATP-dependent oligopeptide transporter that is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Pearce92]. OppABCDF has not been investigated in detail in E. coli, but the orthologous system in Salmonella typhimurium has been extensively characterized. Binding affinity and competition assays have shown that OppABCDF will transport oligopeptides up to five amino acids in length, but has no affinity for free amino acids [Guyer86]. The system has been observed to function in oligopeptide uptake, as well as recycling of cell wall peptides [Hiles87, Goodell87]. Based on sequence similarity, OppB and OppC are the membrane components of the ABC transporter, and OppD and OppF are the ATP-binding components of the ABC transporter [Pearce92]. OppA is the periplasmic substrate-binding component that binds oligopeptides with a Kd of approximately 1E-6 [Tame94]. Insertion mutant of the oppF gene has shown that OppF is required for Opp transporter function [Hiles87]. In addition, insertional mutants of each of the opp genes were constructed, and the opp-minus strains were unable to utilize the peptide Pro-Gly-Gly, normally transported by the wild-type transporter [Hiles87].

OppA has been crystallized and its structure resolved to 2.3 A resolution showing OppA to be a bilobal, principally beta-stranded, three-domain protein [Glover95].

Targeting of OppA to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06].


Enzymatic reaction of: transport of a peptide (peptide ABC transporter OppABCDF)


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 38 -> 59
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Conserved-Region 101 -> 290
[UniProt09]
UniProt: ABC transmembrane type-1;
Transmembrane-Region 103 -> 122
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 140 -> 160
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 164 -> 180
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 216 -> 236
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 268 -> 290
[UniProt10a]
UniProt: Helical;; Non-Experimental Qualifier: probable;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1245 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10676.


References

Andrews86: Andrews JC, Short SA (1986). "opp-lac Operon fusions and transcriptional regulation of the Escherichia coli trp-linked oligopeptide permease." J Bacteriol 1986;165(2);434-42. PMID: 3080404

Angelopoulos96: Angelopoulos N, Kallaras C, Apostolakis M (1996). "Effects of intracerebroventricular administration of atrial natriuretic peptide on subcortical EEG activity in conscious rabbits." Exp Brain Res 1996;108(3);427-32. PMID: 8801122

Baars06: Baars L, Ytterberg AJ, Drew D, Wagner S, Thilo C, van Wijk KJ, de Gier JW (2006). "Defining the role of the Escherichia coli chaperone SecB using comparative proteomics." J Biol Chem 281(15);10024-34. PMID: 16352602

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

Bina03: Bina X, Perreten V, Levy SB (2003). "The periplasmic protein MppA requires an additional mutated locus to repress marA expression in Escherichia coli." J Bacteriol 185(4);1465-9. PMID: 12562820

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

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

Glover95: Glover ID (1995). "Structure determination of OppA at 2.3 A resolution using multiple-wavelength anomalous dispersion methods." Acta Crystallogr D Biol Crystallogr 51(Pt 1);39-47. PMID: 15299334

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

Goodell87: Goodell EW, Higgins CF (1987). "Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli." J Bacteriol 169(8);3861-5. PMID: 3301822

Guyer86: Guyer CA, Morgan DG, Staros JV (1986). "Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli." J Bacteriol 1986;168(2);775-9. PMID: 3536860

Higgins85: Higgins CF, Hiles ID, Whalley K, Jamieson DJ (1985). "Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems." EMBO J 4(4);1033-9. PMID: 3926486

Hiles87: Hiles ID, Gallagher MP, Jamieson DJ, Higgins CF (1987). "Molecular characterization of the oligopeptide permease of Salmonella typhimurium." J Mol Biol 1987;195(1);125-42. PMID: 2821267

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

Lenny80: Lenny AB, Margolin P (1980). "Locations of the opp and supX genes of Salmonella typhimurium and Escherichia coli." J Bacteriol 143(2);747-52. PMID: 7009564

Letoffe06: Letoffe S, Delepelaire P, Wandersman C (2006). "The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins." Proc Natl Acad Sci U S A 103(34);12891-6. PMID: 16905647

Li99e: Li H, Park JT (1999). "The periplasmic murein peptide-binding protein MppA is a negative regulator of multiple antibiotic resistance in Escherichia coli." J Bacteriol 181(16);4842-7. PMID: 10438753

Park93: Park JT (1993). "Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: indirect evidence for an alternative permease system and for a monolayered sacculus." J Bacteriol 175(1);7-11. PMID: 8416911

Park98: Park JT, Raychaudhuri D, Li H, Normark S, Mengin-Lecreulx D (1998). "MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate." J Bacteriol 180(5);1215-23. PMID: 9495761

Pearce92: Pearce SR, Mimmack ML, Gallagher MP, Gileadi U, Hyde SC, Higgins CF (1992). "Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium." Mol Microbiol 1992;6(1);47-57. PMID: 1738314

Polen03: Polen T, Rittmann D, Wendisch VF, Sahm H (2003). "DNA microarray analyses of the long-term adaptive response of Escherichia coli to acetate and propionate." Appl Environ Microbiol 69(3);1759-74. PMID: 12620868

Tame94: Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ (1994). "The structural basis of sequence-independent peptide binding by OppA protein." Science 1994;264(5165);1578-81. PMID: 8202710

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

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470

Other References Related to Gene Regulation

Andrews86a: Andrews JC, Blevins TC, Short SA (1986). "Regulation of peptide transport in Escherichia coli: induction of the trp-linked operon encoding the oligopeptide permease." J Bacteriol 1986;165(2);428-33. PMID: 3511033

Chen07: Chen Z, Lewis KA, Shultzaberger RK, Lyakhov IG, Zheng M, Doan B, Storz G, Schneider TD (2007). "Discovery of Fur binding site clusters in Escherichia coli by information theory models." Nucleic Acids Res 35(20);6762-77. PMID: 17921503

Fraenkel95: Fraenkel YM, Mandel Y, Friedberg D, Margalit H (1995). "Identification of common motifs in unaligned DNA sequences: application to Escherichia coli Lrp regulon." Comput Appl Biosci 1995;11(4);379-87. PMID: 8521047

GamaCastro08: Gama-Castro S, Jimenez-Jacinto V, Peralta-Gil M, Santos-Zavaleta A, Penaloza-Spinola MI, Contreras-Moreira B, Segura-Salazar J, Muniz-Rascado L, Martinez-Flores I, Salgado H, Bonavides-Martinez C, Abreu-Goodger C, Rodriguez-Penagos C, Miranda-Rios J, Morett E, Merino E, Huerta AM, Trevino-Quintanilla L, Collado-Vides J (2008). "RegulonDB (version 6.0): gene regulation model of Escherichia coli K-12 beyond transcription, active (experimental) annotated promoters and Textpresso navigation." Nucleic Acids Res 36(Database issue);D120-4. PMID: 18158297

Higashi08: Higashi K, Terui Y, Suganami A, Tamura Y, Nishimura K, Kashiwagi K, Igarashi K (2008). "Selective Structural Change by Spermidine in the Bulged-out Region of Double-stranded RNA and Its Effect on RNA Function." J Biol Chem 283(47);32989-94. PMID: 18824545

Pulvermacher08: Pulvermacher SC, Stauffer LT, Stauffer GV (2008). "The role of the small regulatory RNA GcvB in GcvB/mRNA posttranscriptional regulation of oppA and dppA in Escherichia coli." FEMS Microbiol Lett 281(1);42-50. PMID: 18312576

Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038

Tao05: Tao H, Hasona A, Do PM, Ingram LO, Shanmugam KT (2005). "Global gene expression analysis revealed an unsuspected deo operon under the control of molybdate sensor, ModE protein, in Escherichia coli." Arch Microbiol 184(4);225-33. PMID: 16205910

Urbanowski00: Urbanowski ML, Stauffer LT, Stauffer GV (2000). "The gcvB gene encodes a small untranslated RNA involved in expression of the dipeptide and oligopeptide transport systems in Escherichia coli." Mol Microbiol 37(4);856-68. PMID: 10972807

Yoshida99: Yoshida M, Meksuriyen D, Kashiwagi K, Kawai G, Igarashi K (1999). "Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon aug in oppa mRNA." J Biol Chem 274(32);22723-8. PMID: 10428855


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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