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Escherichia coli K-12 substr. MG1655 Polypeptide: biotin carboxyl carrier protein



Gene: accB Accession Numbers: EG10275 (EcoCyc), b3255, ECK3242

Synonyms: fabE, apo-[acetyl-CoA:carbon-dioxide ligase (ADP forming)], biotin carboxyl carrier protein monomer, BCCP (monomer)

Regulation Summary Diagram: ?

Regulation summary diagram for accB

Alternative forms of biotin carboxyl carrier protein: biotinylated biotin-carboxyl carrier protein

Summary:
The accB gene encodes the biotin carboxyl carrier protein (BCCP), a component of acetyl CoA carboxylase [Alix89]. AccB is active as a dimer [Cronan01].

The kinetics of the biotinylation reaction have been determined, and the N terminus does not appear to have any role in the modification [Nenortas96]. Biotinylation causes a large structural change in the C-terminal region of the protein [ChapmanSmith97]. Biotinylation results in loss of conformational flexibility of the biotin interaction region [Yao99]; a "thumb" domain comprising amino acids 94-101 fastens the biotin moiety to the surface of the protein [Roberts99a] and this interaction results in increased protein stability [Solbiati02]. This thumb domain is important for acetyl CoA carboxylase activity [Cronan01, Roberts99a]. Unbiotinylated AccB C-terminal domain dimerizes, and biotinylated AccB C-terminal domain is monomeric [ChapmanSmith97].

AccB appears to interact with the C terminus of the BirA biotin ligase [ChapmanSmith01]. The interaction of BirA with AccB BirA-BCCP binding may preclude BirA dimerization and therefore DNA binding and transcriptional repressor activity of BirA [Weaver01].

A crystal structure of the biotinyl domain is presented at 1.8 angstrom resolution [Athappilly95]. An NMR structure of the C-terminal domain has also been determined [Yao97, Roberts99a] and implications with respect to specificity of protein-protein interactions are discussed [Yao97]. Structural characterization of biotin carboxyl carrier protein (BCCP) by circular dichroism indicates that the biotin moiety may be partly engulfed within the protein rather than fully exposed in solution [Fall76]. Secondary structure predictions have been made [Toh93].

Mutation of the MKM biotinylation sequence reveals substrate requirements; the position of the lysine is critical and the flanking methionines are not [Reche98]. Production of a protein with a mutation of the biotinylated lysine residue partially complements the heat sensitivity of another accB mutant, probably due to formation of mutant heterodimers [Cronan01]. A fabE/accB mutation is shown to disrupt biotinylation [Li92]. E119K and E147K mutant proteins exhibit defects in biotinylation that are due to defects in interaction with BirA, the biotin ligase [ChapmanSmith99]. Mutation of residue G133, G143, or V146 causes structural disruption of the protein [ChapmanSmith99]. A linker region N-terminal to the biotinoyl domain is also essential for function (but not required for biotinylation) [Cronan02a]. Mutations in accB or accC suppress the inviability of an htrB mutant at 42 deg, which is due to accumulation of excess phospholipids [Karow92].

AccB has 57% identity to Anabaena sp. strain PCC 7120 biotin carboxyl carrier protein [Gornicki93] and has similarity to biotin carboxyl carrier proteins from Pseudomonas aeruginosa [Best93], Mycobacterium leprae [Norman94], Mycobacterium tuberculosis [Norman94], Bacillus subtilis [Marini95], Glycine max (soybean) [Reverdatto99], Sulfolobus metallicus [Burton99], Lactobacillus plantarum [Kiatpapan01], Arabidopsis thaliana [Thelen01], and Aquifex aeolicus [Clarke03]. AccB has similarity to the putative protein encoded by ORF2 of Lactobacillus sanfranciscensis DSM20451T [Ehrmann98]. AccB also has similarity to Streptomyces venezuelae ISP5230 JadJ protein, which is involved in biosynthesis of the polyketide antibiotic jadomycin B [Han00]. Pseudomonas aeruginosa AccB functionally complements conditional lethality of an accB mutation in E. coli[Best93].

AccB exhibits an abnormally large apparent molecular weight of 22.5 kDa, compared to the predicted molecular weight of about 16.7 kDa [Li92].

Purification of AccB is described [Nenortas96].

AccB peptides have been fused to exogenous proteins for use as biotinylation signals that facilitate purification [Weiss94, Sibler99].

Reviews: [Cronan02, ChapmanSmith99a].

Citations: [Wachi87, Muramatsu89, ChapmanSmith94]

Gene Citations: [Li93]

Locations: cytosol

Map Position: [3,403,458 -> 3,403,928] (73.36 centisomes, 264°)
Length: 471 bp / 156 aa

Molecular Weight of Polypeptide: 16.687 kD (from nucleotide sequence), 22.5 kD (experimental)

pI: 4.74

Unification Links: ASAP:ABE-0010675 , CGSC:796 , DIP:DIP-48007N , DisProt:DP00415 , EchoBASE:EB0271 , EcoGene:EG10275 , EcoliWiki:b3255 , Mint:MINT-1292848 , ModBase:P0ABD8 , OU-Microarray:b3255 , PortEco:accB , PR:PRO_000022033 , Pride:P0ABD8 , Protein Model Portal:P0ABD8 , RegulonDB:EG10275 , SMR:P0ABD8 , String:511145.b3255 , UniProt:P0ABD8

Relationship Links: InterPro:IN-FAMILY:IPR000089 , InterPro:IN-FAMILY:IPR001249 , InterPro:IN-FAMILY:IPR001882 , InterPro:IN-FAMILY:IPR011053 , PDB:Structure:1A6X , PDB:Structure:1BDO , PDB:Structure:1K67 , PDB:Structure:1K69 , PDB:Structure:2BDO , PDB:Structure:3BDO , PDB:Structure:4HR7 , Pfam:IN-FAMILY:PF00364 , Prints:IN-FAMILY:PR01071 , Prosite:IN-FAMILY:PS00188 , Prosite:IN-FAMILY:PS50968

Reactions known to consume the compound:

biotin-carboxyl carrier protein assembly :
a [biotin-carboxyl-carrier protein monomer] + biotin + ATP → AMP + a biotinylated [BCCP monomer] + diphosphate + H+

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for accB

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a, Davis00]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003989 - acetyl-CoA carboxylase activity Inferred from experiment Inferred by computational analysis [GOA01a, Davis00]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06, Butland05]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by curator [Davis00]
GO:0009317 - acetyl-CoA carboxylase complex Inferred by computational analysis [GOA01a]

MultiFun Terms: metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers biotin carboxyl carrier protein

Essentiality data for accB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Sequence Features

Protein sequence of biotin carboxyl carrier protein with features indicated

Feature Class Location Citations Comment
Conserved-Region 73 -> 156
[UniProt14]
UniProt: Biotinyl-binding.
Sequence-Conflict 113
[Alix89, UniProt10a]
UniProt: (in Ref. 2);
N6-biotinyllysine-Modification 122
[Sutton77, UniProt15]
UniProt: N6-biotinyllysine.


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram

Notes:

History:
10/20/97 Gene b3255 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10275; confirmed by SwissProt match.


References

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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

Athappilly95: Athappilly FK, Hendrickson WA (1995). "Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing." Structure 3(12);1407-19. PMID: 8747466

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

Best93: Best EA, Knauf VC (1993). "Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase." J Bacteriol 175(21);6881-9. PMID: 7693652

Burton99: Burton NP, Williams TD, Norris PR (1999). "Carboxylase genes of Sulfolobus metallicus." Arch Microbiol 172(6);349-53. PMID: 10591844

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

ChapmanSmith01: Chapman-Smith A, Mulhern TD, Whelan F, Cronan JE, Wallace JC (2001). "The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity." Protein Sci 10(12);2608-17. PMID: 11714929

ChapmanSmith94: Chapman-Smith A, Turner DL, Cronan JE, Morris TW, Wallace JC (1994). "Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase." Biochem J 302 ( Pt 3);881-7. PMID: 7945216

ChapmanSmith97: Chapman-Smith A, Forbes BE, Wallace JC, Cronan JE (1997). "Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase." J Biol Chem 272(41);26017-22. PMID: 9325338

ChapmanSmith99: Chapman-Smith A, Morris TW, Wallace JC, Cronan JE (1999). "Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase." J Biol Chem 274(3);1449-57. PMID: 9880519

ChapmanSmith99a: Chapman-Smith A, Cronan JE (1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity." Trends Biochem Sci 24(9);359-63. PMID: 10470036

Clarke03: Clarke DJ, Coulson J, Baillie R, Campopiano DJ (2003). "Biotinylation in the hyperthermophile Aquifex aeolicus." Eur J Biochem 270(6);1277-87. PMID: 12631286

Cronan01: Cronan JE (2001). "The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure id essential and that the domain functions as a dimer." J Biol Chem 276(40);37355-64. PMID: 11495922

Cronan02: Cronan JE, Waldrop GL (2002). "Multi-subunit acetyl-CoA carboxylases." Prog Lipid Res 41(5);407-35. PMID: 12121720

Cronan02a: Cronan JE (2002). "Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase." J Biol Chem 277(25);22520-7. PMID: 11956202

Davis00: Davis MS, Solbiati J, Cronan JE (2000). "Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli." J Biol Chem 275(37);28593-8. PMID: 10893421

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

Ehrmann98: Ehrmann MA, Vogel RF (1998). "Maltose metabolism of Lactobacillus sanfranciscensis: cloning and heterologous expression of the key enzymes, maltose phosphorylase and phosphoglucomutase." FEMS Microbiol Lett 169(1);81-6. PMID: 9851037

Fall76: Fall RR, Glaser M, Vagelos PR (1976). "Acetyl coenzyme A carbosylase. Circular dichroism studies of Escherichia coli biotin carboxyl carrier protein." J Biol Chem 251(7);2063-9. PMID: 5438

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

Gornicki93: Gornicki P, Scappino LA, Haselkorn R (1993). "Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena sp. strain PCC 7120: biotin carboxylase and biotin carboxyl carrier protein." J Bacteriol 175(16);5268-72. PMID: 8102363

Han00: Han L, Yang K, Kulowski K, Wendt-Pienkowski E, Hutchinson CR, Vining LC (2000). "An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230." Microbiology 146 ( Pt 4);903-10. PMID: 10784049

Karow92: Karow M, Fayet O, Georgopoulos C (1992). "The lethal phenotype caused by null mutations in the Escherichia coli htrB gene is suppressed by mutations in the accBC operon, encoding two subunits of acetyl coenzyme A carboxylase." J Bacteriol 174(22);7407-18. PMID: 1358874

Kiatpapan01: Kiatpapan P, Kobayashi H, Sakaguchi M, Ono H, Yamashita M, Kaneko Y, Murooka Y (2001). "Molecular characterization of Lactobacillus plantarum genes for beta-ketoacyl-acyl carrier protein synthase III (fabH) and acetyl coenzyme A carboxylase (accBCDA), which are essential for fatty acid biosynthesis." Appl Environ Microbiol 67(1);426-33. PMID: 11133475

Li92: Li SJ, Cronan JE (1992). "The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase." J Biol Chem 267(2);855-63. PMID: 1370469

Li93: Li SJ, Cronan JE (1993). "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis." J Bacteriol 1993;175(2);332-40. PMID: 7678242

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

Marini95: Marini P, Li SJ, Gardiol D, Cronan JE, de Mendoza D (1995). "The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis." J Bacteriol 177(23);7003-6. PMID: 7592499

Muramatsu89: Muramatsu S, Mizuno T (1989). "Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli." Nucleic Acids Res 17(10);3982. PMID: 2660106

Nenortas96: Nenortas E, Beckett D (1996). "Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase." J Biol Chem 271(13);7559-67. PMID: 8631788

Norman94: Norman E, De Smet KA, Stoker NG, Ratledge C, Wheeler PR, Dale JW (1994). "Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis." J Bacteriol 176(9);2525-31. PMID: 7909542

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

Reche98: Reche P, Li YL, Fuller C, Eichhorn K, Perham RN (1998). "Selectivity of post-translational modification in biotinylated proteins: the carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli." Biochem J 329 ( Pt 3);589-96. PMID: 9445386

Reverdatto99: Reverdatto S, Beilinson V, Nielsen NC (1999). "A multisubunit acetyl coenzyme A carboxylase from soybean." Plant Physiol 119(3);961-78. PMID: 10069834

Roberts99a: Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE, Perham RN (1999). "Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy." Biochemistry 38(16);5045-53. PMID: 10213607

Sibler99: Sibler AP, Kempf E, Glacet A, Orfanoudakis G, Bourel D, Weiss E (1999). "In vivo biotinylated recombinant antibodies: high efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments." J Immunol Methods 224(1-2);129-40. PMID: 10357213

Solbiati02: Solbiati J, Chapman-Smith A, Cronan JE (2002). "Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure." J Biol Chem 277(24);21604-9. PMID: 11943781

Sutton77: Sutton MR, Fall RR, Nervi AM, Alberts AW, Vagelos PR, Bradshaw RA (1977). "Amino acid sequence of Escherichia coli biotin carboxyl carrier protein (9100)." J Biol Chem 1977;252(11);3934-40. PMID: 324999

Thelen01: Thelen JJ, Mekhedov S, Ohlrogge JB (2001). "Brassicaceae express multiple isoforms of biotin carboxyl carrier protein in a tissue-specific manner." Plant Physiol 125(4);2016-28. PMID: 11299381

Toh93: Toh H, Kondo H, Tanabe T (1993). "Molecular evolution of biotin-dependent carboxylases." Eur J Biochem 215(3);687-96. PMID: 8102604

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-08 released on 2014-08-01 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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."

Wachi87: Wachi M, Doi M, Tamaki S, Park W, Nakajima-Iijima S, Matsuhashi M (1987). "Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli." J Bacteriol 169(11);4935-40. PMID: 2822655

Weaver01: Weaver LH, Kwon K, Beckett D, Matthews BW (2001). "Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor." Protein Sci 10(12);2618-22. PMID: 11714930

Weiss94: Weiss E, Chatellier J, Orfanoudakis G (1994). "In vivo biotinylated recombinant antibodies: construction, characterization, and application of a bifunctional Fab-BCCP fusion protein produced in Escherichia coli." Protein Expr Purif 5(5);509-17. PMID: 7827508

Yao97: Yao X, Wei D, Soden C, Summers MF, Beckett D (1997). "Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase." Biochemistry 36(49);15089-100. PMID: 9398236

Yao99: Yao X, Soden C, Summers MF, Beckett D (1999). "Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase." Protein Sci 8(2);307-17. PMID: 10048324

Other References Related to Gene Regulation

James04: James ES, Cronan JE (2004). "Expression of two Escherichia coli acetyl-CoA carboxylase subunits is autoregulated." J Biol Chem 279(4);2520-7. PMID: 14594796

Vanet93: Vanet A, Plumbridge JA, Alix JH (1993). "Cotranscription of two genes necessary for ribosomal protein L11 methylation (prmA) and pantothenate transport (panF) in Escherichia coli K-12." J Bacteriol 1993;175(22);7178-88. PMID: 8226664


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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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