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Escherichia coli K-12 substr. MG1655 Polypeptide: ferric enterobactin ABC transporter - membrane subunit



Gene: fepG Accession Numbers: EG10298 (EcoCyc), b0589, ECK0582

Regulation Summary Diagram: ?

Component of:
ferric enterobactin ABC transporter (extended summary available)
ferric enterobactin transport system (summary available)

Gene Citations: [Shea91]

Locations: inner membrane

Map Position: [619,419 <- 620,411] (13.35 centisomes)
Length: 993 bp / 330 aa

Molecular Weight of Polypeptide: 34.91 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0002027 , CGSC:31162 , DIP:DIP-9597N , EchoBASE:EB0294 , EcoGene:EG10298 , EcoliWiki:b0589 , ModBase:P23877 , OU-Microarray:b0589 , PortEco:fepG , PR:PRO_000022605 , Pride:P23877 , Protein Model Portal:P23877 , RefSeq:NP_415121 , RegulonDB:EG10298 , SMR:P23877 , String:511145.b0589 , UniProt:P23877

Relationship Links: InterPro:IN-FAMILY:IPR000522 , Pfam:IN-FAMILY:PF01032

In Paralogous Gene Group: 53 (5 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0055072 - iron ion homeostasis Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005215 - transporter activity Inferred by computational analysis [GOA01]
GO:0015623 - iron-chelate-transporting ATPase activity Inferred by computational analysis
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes adaptations Fe aquisition
cell structure membrane
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 fepG 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: ferric enterobactin ABC transporter

Subunit composition of ferric enterobactin ABC transporter = [FepC]2[FepD][FepG][FepB]
         ferric enterobactin ABC transporter - ATP binding subunit = FepC (extended summary available)
         ferric enterobactin ABC transporter - membrane subunit = FepD
         ferric enterobactin ABC transporter - membrane subunit = FepG
         ferric enterobactin ABC transporter - periplasmic binding protein = FepB

Component of: ferric enterobactin transport system (summary available)

Summary:
FepBCDG are components of a ferric enterobactin transport complex that is a member of the ATP-binding cassette (ABC) family of transporters. E. coli and several other species of Enterobacteriaceae secrete the catecholate siderophore enterobactin. The enterobactin siderophore is a small organic molecule with a high affinity for Fe 3+. FepA has been shown [Barnard01], to be involved in transport of ferric enterobactin across the outer membrane into the periplasm in a TonB-dependent process which requires the transduction of energy derived from the cytoplasmic membrane across the periplasm to FepA. Deletion studies [Shea91] indicate that fepD and fepG are essential for transport and sequence analysis indicates that these two proteins are highly homologous with other integral membrane proteins involved in iron-chelating ABC uptake systems. Based on sequence similarity, FepC is the ATP-binding component and provides the energy required for transport across the inner membrane. FepB is not coded in the same operon but has been shown to bind ferric enterobactin and probably functions as the periplasmic binding protein of the ferric enterobactin ABC transporter [Stephens95].


Enzymatic reaction of: transport of ferric enterobactin (ferric enterobactin ABC transporter)

EC Number: 3.6.3.34

Alternative Products for ferric enterobactin complex: ferric (2,3-dihydroxybenzoylserine)3 [Hantke90 ]


Subunit of: ferric enterobactin transport system

Subunit composition of ferric enterobactin transport system = [(FepC)2(FepD)(FepG)(FepB)][([TonB][ExbB][ExbD])(FepA)]
         ferric enterobactin ABC transporter = (FepC)2(FepD)(FepG)(FepB) (extended summary available)
                 ferric enterobactin ABC transporter - ATP binding subunit = FepC (extended summary available)
                 ferric enterobactin ABC transporter - membrane subunit = FepD
                 ferric enterobactin ABC transporter - membrane subunit = FepG
                 ferric enterobactin ABC transporter - periplasmic binding protein = FepB
         ferric enterobactin outer membrane transport complex = ([TonB][ExbB][ExbD])(FepA)
                 TonB energy transducing system = (TonB)(ExbB)(ExbD) (extended summary available)
                         TonB energy transducing system - TonB subunit = TonB (extended summary available)
                         TonB energy transducing system - ExbB subunit = ExbB (summary available)
                         tonB energy transducing system - ExbD subunit = ExbD (summary available)
                 ferric enterobactin / colicin B / colicin D outer membrane porin FepA = FepA (summary available)

Summary:
FepA is a 22-stranded membrane-spanning beta barrel protein in the outer membrane. FepA is a TonB dependent active transporter that recognizes ferric enterobactin and translocates the molecule across the outer membrane into the periplasm. FepB is a periplasmic binding protein that binds ferric enterobactin for transport across the inner membrane by the FepCDG ABC transporter.

Locations: outer membrane, inner membrane, periplasmic space

GO Terms:

Cellular Component: GO:0005886 - plasma membrane
GO:0009279 - cell outer membrane
GO:0030288 - outer membrane-bounded periplasmic space


Enzymatic reaction of: ferric enterobactin transport


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 8 -> 28
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 63 -> 83
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 93 -> 113
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 118 -> 138
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 147 -> 167
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 191 -> 211
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 230 -> 231
[Shea91, UniProt10a]
Alternate sequence: SV → RL; UniProt: (in Ref. 1; CAA40708);
Transmembrane-Region 236 -> 256
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 276 -> 296
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 304 -> 324
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0589 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10298; confirmed by SwissProt match.


References

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

Barnard01: Barnard TJ, Watson ME, McIntosh MA (2001). "Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport." Mol Microbiol 2001;41(3);527-36. PMID: 11532122

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

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

Hantke90: Hantke K (1990). "Dihydroxybenzoylserine--a siderophore for E. coli." FEMS Microbiol Lett 55(1-2);5-8. PMID: 2139424

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

Pugsley76: Pugsley AP, Reeves P (1976). "Iron uptake in colicin B-resistant mutants of Escherichia coli K-12." J Bacteriol 126(3);1052-62. PMID: 7543

Shea91: Shea CM, McIntosh MA (1991). "Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli." Mol Microbiol 1991;5(6);1415-28. PMID: 1838574

Skare93: Skare JT, Ahmer BM, Seachord CL, Darveau RP, Postle K (1993). "Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA." J Biol Chem 268(22);16302-8. PMID: 8344918

Sprencel00: Sprencel C, Cao Z, Qi Z, Scott DC, Montague MA, Ivanoff N, Xu J, Raymond KM, Newton SM, Klebba PE (2000). "Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB." J Bacteriol 182(19);5359-64. PMID: 10986237

Stephens95: Stephens DL, Choe MD, Earhart CF (1995). "Escherichia coli periplasmic protein FepB binds ferrienterobactin." Microbiology 1995;141 ( Pt 7);1647-54. PMID: 7551033

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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."

Other References Related to Gene Regulation

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

Chenault91: Chenault SS, Earhart CF (1991). "Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease." Mol Microbiol 1991;5(6);1405-13. PMID: 1787794

Christoffersen01: Christoffersen CA, Brickman TJ, Hook-Barnard I, McIntosh MA (2001). "Regulatory architecture of the iron-regulated fepD-ybdA bidirectional promoter region in Escherichia coli." J Bacteriol 183(6);2059-70. PMID: 11222606

Lavrrar02: Lavrrar JL, Christoffersen CA, McIntosh MA (2002). "Fur-DNA interactions at the bidirectional fepDGC-entS promoter region in Escherichia coli." J Mol Biol 322(5);983-95. PMID: 12367523


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 Sun Nov 23, 2014, BIOCYC14A.