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Escherichia coli K-12 substr. MG1655 Transporter: maltose outer membrane porin / phage lambda receptor protein



Gene: lamB Accession Numbers: EG10528 (EcoCyc), b4036, ECK4028

Synonyms: malL, malB, maltoporin, maltose high-affinity receptor, phage lambda receptor protein

Regulation Summary Diagram: ?

Subunit composition of maltose outer membrane porin / phage lambda receptor protein = [LamB]3

Summary:
LamB is a member of the Sugar Porin (SP) family. It specifically facilitates the diffusion of maltose and other maltodextrins (α1-4 linked polyglucosyls) across the outer membrane [Wang97g].

LamB was originally discovered as a receptor for the bacteriophage lambda [RandallHazelbau73]. X-ray crystallography suggests an 18-stranded antiparallel beta-barrel structure forms the channel [Schirmer95]. In order to facillitate diffusion of malodextrins, it must form a homotrimer [Schirmer95]. Targeting of LamB to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06]. Proteomic studies indicate that LamB is an important outer membrane protein for tetracycline resistance in E. coli [Zhang08].

Reviews: [Charbit03, Klebba02]

Citations: [Ferenci80a, Ferenci80b, Benz86, Dutzler96, Van01a, Denker05]

Gene Citations: [Rousset86]

Locations: outer membrane

Map Position: [4,245,994 -> 4,247,334] (91.51 centisomes)
Length: 1341 bp / 446 aa

Molecular Weight of Polypeptide: 49.912 kD (from nucleotide sequence), 47.0 kD (experimental) [Luckey80 ]

Unification Links: ASAP:ABE-0013218 , CGSC:575 , DIP:DIP-10082N , EchoBASE:EB0523 , EcoGene:EG10528 , EcoliWiki:b4036 , ModBase:P02943 , OU-Microarray:b4036 , PortEco:lamB , PR:PRO_000023072 , Pride:P02943 , Protein Model Portal:P02943 , RefSeq:NP_418460 , RegulonDB:EG10528 , SMR:P02943 , String:511145.b4036 , UniProt:P02943

Relationship Links: InterPro:IN-FAMILY:IPR003192 , InterPro:IN-FAMILY:IPR023738 , PDB:Structure:1AF6 , PDB:Structure:1MAL , PDB:Structure:1MPM , PDB:Structure:1MPN , PDB:Structure:1MPO , PDB:Structure:1MPQ , Pfam:IN-FAMILY:PF02264 , ProDom:IN-FAMILY:PD008788

In Paralogous Gene Group: 553 (2 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0042956 - maltodextrin transport Inferred from experiment Inferred by computational analysis [GOA01a, Luckey80]
GO:0055085 - transmembrane transport Inferred by computational analysis Inferred from experiment [Schirmer95, UniProtGOA11a, GOA06]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a]
GO:0009615 - response to virus Inferred by computational analysis [UniProtGOA11a]
GO:0015768 - maltose transport Inferred by computational analysis [GOA06, GOA01a]
GO:0016032 - viral process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Gelis07]
GO:0015288 - porin activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, Schirmer95]
GO:0042958 - maltodextrin transmembrane transporter activity Inferred from experiment Inferred by computational analysis [GOA01a, Luckey80]
GO:0001618 - virus receptor activity Inferred by computational analysis [UniProtGOA11a]
GO:0015481 - maltose transporting porin activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, DiazMejia09, Han12, Molloy00, LopezCampistrou05, Luckey80]
GO:0045203 - integral component of cell outer membrane Inferred from experiment [Luckey80]
GO:0046930 - pore complex Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Schirmer95]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: extrachromosomal prophage genes and phage related functions
transport Channel-type Transporters Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily)

Essentiality data for lamB 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:
Created 06-Dec-2007 by Johnson A , JCVI


Enzymatic reaction of: Transport of maltose (maltose outer membrane porin / phage lambda receptor protein)


Enzymatic reaction of: Transport of non-specific ion/solute (maltose outer membrane porin / phage lambda receptor protein)


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 25
[UniProt10]
Chain 26 -> 446
[UniProt09]
UniProt: Maltoporin;
Transmembrane-Region 27 -> 35
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Site 31
[UniProt10]
UniProt: Greasy slide, important in sugar transport; Sequence Annotation Type: site;
Mutagenesis-Variant 33
[Heine87, UniProt11]
Alternate sequence: R → H; UniProt: Reduces ligand affinity and pore size, no longer selective for maltodextrins.
Sequence-Conflict 35
[Heine88, UniProt10]
Alternate sequence: G → GSG; UniProt: (in Ref. 8);
Disulfide-Bond-Site 63, 47
[Luckey91, UniProt11]
.
Transmembrane-Region 65 -> 78
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Site 66
[UniProt10]
UniProt: Greasy slide, important in sugar transport; Sequence Annotation Type: site;
Transmembrane-Region 81 -> 93
[UniProt10]
UniProt: Beta stranded;
Mutagenesis-Variant 99
[Heine87, UniProt11]
Alternate sequence: W → R; UniProt: Decreases starch affinity, slightly increases maltose affinity.
Amino-Acid-Site 99
[UniProt10]
UniProt: Greasy slide, important in sugar transport; Sequence Annotation Type: site;
Transmembrane-Region 105 -> 115
[UniProt10]
UniProt: Beta stranded;
Mutagenesis-Variant 107
[Heine87, UniProt11]
Alternate sequence: R → S; UniProt: Decreases maltodextrin affinity, increases sucrose binding and transport.
Transmembrane-Region 123 -> 130
[UniProt10]
UniProt: Beta stranded;
Mutagenesis-Variant 134
[Van01a, UniProt11]
Alternate sequence: R → N; UniProt: Slight increase in pore size; increase in sucrose transport and slight decrease in maltose transport; when associated with D-143 and F-146.
Alternate sequence: R → D; UniProt: Slight increase in pore size; increase in sucrose transport and slight decrease in maltose transport; when associated with D-143 and F-146.
Alternate sequence: R → A; UniProt: Considerable increase in pore size and sucrose transport, slight decrease in maltose transport; when associated with A-143.
Mutagenesis-Variant 143
[Van01a, Heine87, UniProt11]
Alternate sequence: Y → F; UniProt: Increases affinity for starch and maltose, pore size and transport of maltohexaose.
Amino-Acid-Site 143
[UniProt10]
UniProt: Important in sugar transport; Sequence Annotation Type: site;
Mutagenesis-Variant 146
[Van01a, Heine87, UniProt11]
Alternate sequence: D → G; UniProt: Increases affinity for large dextrins.
Transmembrane-Region 149 -> 159
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 162 -> 173
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 192 -> 205
[UniProt10]
UniProt: Beta stranded;
Sequence-Conflict 208
[Heine88, UniProt10]
Alternate sequence: P → PDP; UniProt: (in Ref. 8);
Transmembrane-Region 210 -> 222
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 235 -> 248
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 251 -> 263
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Site 252
[UniProt10]
UniProt: Greasy slide, important in sugar transport; Sequence Annotation Type: site;
Transmembrane-Region 291 -> 305
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 308 -> 323
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 327 -> 341
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 344 -> 359
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 363 -> 378
[UniProt10]
UniProt: Beta stranded;
Sequence-Conflict 381
[Blattner93, UniProt10]
Alternate sequence: S → T; UniProt: (in Ref. 2; AAC43130);
Amino-Acid-Site 383
[UniProt10]
UniProt: Greasy slide, important in sugar transport; Sequence Annotation Type: site;
Sequence-Conflict 385
[Heine88, UniProt10]
Alternate sequence: R → RDP; UniProt: (in Ref. 8);
Transmembrane-Region 386 -> 400
[UniProt10]
UniProt: Beta stranded;
Transmembrane-Region 431 -> 445
[UniProt10]
UniProt: Beta stranded;
Amino-Acid-Site 445
[UniProt10]
UniProt: Greasy slide, important in sugar transport; Sequence Annotation Type: site;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b4036 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10528; confirmed by SwissProt match.


References

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

Benz86: Benz R, Schmid A, Nakae T, Vos-Scheperkeuter GH (1986). "Pore formation by LamB of Escherichia coli in lipid bilayer membranes." J Bacteriol 165(3);978-86. PMID: 2419312

Blattner93: Blattner FR, Burland V, Plunkett G, Sofia HJ, Daniels DL (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 1993;21(23);5408-17. PMID: 8265357

Charbit03: Charbit A (2003). "Maltodextrin transport through lamb." Front Biosci 8;s265-74. PMID: 12700071

Denker05: Denker K, Orlik F, Schiffler B, Benz R (2005). "Site-directed mutagenesis of the greasy slide aromatic residues within the LamB (maltoporin) channel of Escherichia coli: effect on ion and maltopentaose transport." J Mol Biol 352(3);534-50. PMID: 16095613

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

Dutzler96: Dutzler R, Wang YF, Rizkallah P, Rosenbusch JP, Schirmer T (1996). "Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway." Structure 4(2);127-34. PMID: 8805519

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

Ferenci80a: Ferenci T, Boos W (1980). "The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins." J Supramol Struct 13(1);101-16. PMID: 7003263

Ferenci80b: Ferenci T, Brass J, Boos W (1980). "The role of the periplasmic maltose-binding protein and the outer-membrane phage lambda receptor in maltodextrin transport of Escherichia coli." Biochem Soc Trans 8(6);680-1. PMID: 6450701

Gelis07: Gelis I, Bonvin AM, Keramisanou D, Koukaki M, Gouridis G, Karamanou S, Economou A, Kalodimos CG (2007). "Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR." Cell 131(4);756-69. PMID: 18022369

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

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

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Han12: Han MJ, Lee SY, Hong SH (2012). "Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains." J Microbiol Biotechnol 22(4);470-8. PMID: 22534293

Heine87: Heine HG, Kyngdon J, Ferenci T (1987). "Sequence determinants in the lamB gene of Escherichia coli influencing the binding and pore selectivity of maltoporin." Gene 53(2-3);287-92. PMID: 3301537

Heine88: Heine HG, Francis G, Lee KS, Ferenci T (1988). "Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure." J Bacteriol 170(4);1730-8. PMID: 2832377

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

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Klebba02: Klebba PE (2002). "Mechanism of maltodextrin transport through LamB." Res Microbiol 153(7);417-24. PMID: 12405347

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Luckey80: Luckey M, Nikaido H (1980). "Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli." Proc Natl Acad Sci U S A 77(1);167-71. PMID: 6444720

Luckey91: Luckey M, Ling R, Dose A, Malloy B (1991). "Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane." J Biol Chem 266(3);1866-71. PMID: 1988451

Molloy00: Molloy MP, Herbert BR, Slade MB, Rabilloud T, Nouwens AS, Williams KL, Gooley AA (2000). "Proteomic analysis of the Escherichia coli outer membrane." Eur J Biochem 267(10);2871-81. PMID: 10806384

Nakae80: Nakae T, Ishii J (1980). "Permeability properties of Escherichia coli outer membrane containing, pore-forming proteins: comparison between lambda receptor protein and porin for saccharide permeation." J Bacteriol 142(3);735-40. PMID: 6247333

RandallHazelbau73: Randall-Hazelbauer L, Schwartz M (1973). "Isolation of the bacteriophage lambda receptor from Escherichia coli." J Bacteriol 1973;116(3);1436-46. PMID: 4201774

Rousset86: Rousset JP, Gilson E, Hofnung M (1986). "malM, a new gene of the maltose regulon in Escherichia coli K12. II. Mutations affecting the signal peptide of the MalM protein." J Mol Biol 1986;191(3);313-20. PMID: 3102747

Schirmer95: Schirmer T, Keller TA, Wang YF, Rosenbusch JP (1995). "Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution." Science 1995;267(5197);512-4. PMID: 7824948

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.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 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."

Van01a: Van Gelder P, Dutzler R, Dumas F, Koebnik R, Schirmer T (2001). "Sucrose transport through maltoporin mutants of Escherichia coli." Protein Eng 14(11);943-8. PMID: 11742115

Wang97g: Wang YF, Dutzler R, Rizkallah PJ, Rosenbusch JP, Schirmer T (1997). "Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin." J Mol Biol 1997;272(1);56-63. PMID: 9299337

Zhang08: Zhang DF, Jiang B, Xiang ZM, Wang SY (2008). "Functional characterisation of altered outer membrane proteins for tetracycline resistance in Escherichia coli." Int J Antimicrob Agents 32(4);315-9. PMID: 18620846

Other References Related to Gene Regulation

Boos98: Boos W, Shuman H (1998). "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation." Microbiol Mol Biol Rev 62(1);204-29. PMID: 9529892

Gogol11: Gogol EB, Rhodius VA, Papenfort K, Vogel J, Gross CA (2011). "Small RNAs endow a transcriptional activator with essential repressor functions for single-tier control of a global stress regulon." Proc Natl Acad Sci U S A 108(31);12875-80. PMID: 21768388

Merkel92: Merkel TJ, Nelson DM, Brauer CL, Kadner RJ (1992). "Promoter elements required for positive control of transcription of the Escherichia coli uhpT gene." J Bacteriol 1992;174(9);2763-70. PMID: 1569008

Raibaud89: Raibaud O (1989). "Nucleoprotein structures at positively regulated bacterial promoters: homology with replication origins and some hypotheses on the quaternary structure of the activator proteins in these complexes." Mol Microbiol 1989;3(3);455-8. PMID: 2664421

Raibaud89a: Raibaud O, Vidal-Ingigliardi D, Richet E (1989). "A complex nucleoprotein structure involved in activation of transcription of two divergent Escherichia coli promoters." J Mol Biol 1989;205(3);471-85. PMID: 2538630

Richet00: Richet E (2000). "Synergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP." EMBO J 19(19);5222-32. PMID: 11013224

Richet91: Richet E, Raibaud O (1991). "Supercoiling is essential for the formation and stability of the initiation complex at the divergent malEp and malKp promoters." J Mol Biol 218(3);529-42. PMID: 2016744

Richet96: Richet E (1996). "On the role of the multiple regulatory elements involved in the activation of the Escherichia coli malEp promoter." J Mol Biol 264(5);852-62. PMID: 9000616

VidalIngigliard91: Vidal-Ingigliardi D, Raibaud O (1991). "Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters." Proc Natl Acad Sci U S A 1991;88(1);229-33. PMID: 1824723


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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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