RegulonDB RegulonDB 10.8: Gene Form
   

metG gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

metG mrp yehF LexA RcsB-BglJ anti-anti-terminator anti-terminator terminator yehFp yehFp metGp metGp TSS_2441 TSS_2441 mrpp mrpp TSS_2440 (cluster) TSS_2440 (cluster) TSS_2439 (cluster) TSS_2439 (cluster) TSS_2438 TSS_2438 mrpp7 mrpp7 mrpp2 mrpp2 metGp2 metGp2

Gene      
Name: metG    Texpresso search in the literature
Synonym(s): ECK2107, EG10586, b2114
Genome position(nucleotides): 2194300 --> 2196333 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
53.05
External database links:  
ASAP:
ABE-0006991
CGSC:
510
ECHOBASE:
EB0581
MIM:
615486
MIM:
616280
OU-MICROARRAY:
b2114
PortEco:
metG
STRING:
511145.b2114
COLOMBOS: metG


Product      
Name: methionine—tRNA ligase
Synonym(s): MetG, MetRS
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 76.255
Isoelectric point: 5.652
Motif(s):
 
Type Positions Sequence
2 -> 677 TQVAKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK
336 -> 336 K
575 -> 677 DFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK
581 -> 674 LRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGH
8 -> 397 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.1 - amino acid -activation
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0005515 - protein binding
GO:0046872 - metal ion binding
GO:0016874 - ligase activity
GO:0004812 - aminoacyl-tRNA ligase activity
GO:0003723 - RNA binding
GO:0000049 - tRNA binding
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0008270 - zinc ion binding
GO:0004825 - methionine-tRNA ligase activity
GO:0042803 - protein homodimerization activity
biological_process GO:0006412 - translation
GO:0006418 - tRNA aminoacylation for protein translation
GO:0006431 - methionyl-tRNA aminoacylation
Note(s): Note(s): ...[more].
Reference(s): [1] Abdeljabbar DM., et al., 2009
[2] Armstrong JB., et al., 1975
[3] Barker DG., et al., 1982
[4] Berne PF., et al., 1990
[5] Blanquet S., et al., 1976
[6] Bruton C., et al., 1975
[7] Bruton CJ., et al., 1970
[8] Bruton CJ., et al., 1974
[9] Cassio D. 1968
[10] Cassio D., et al., 1970
[11] Cassio D., et al., 1971
[12] Cassio D., et al., 1968
[13] Cassio D., et al., 1971
[14] Dardel F., et al., 1991
[15] Dessen P., et al., 1982
[16] Dessen P., et al., 1985
[17] Dube SK. 1973
[18] Fayat G., et al., 1977
[19] Fayat G., et al., 1979
[20] Gillet S., et al., 1997
[21] Graffe M., et al., 1992
[22] Gulik A., et al., 1976
[23] Hirel PH., et al., 1988
[24] Hountondji C., et al., 1979
[25] Hountondji C., et al., 1986
[26] Jakubowski H. 2000
[27] Jakubowski H. 2002
[28] Jakubowski H. 1993
[29] Kabir MM., et al., 2001
[30] Kalogerakos T., et al., 1979
[31] Kalogerakos T., et al., 1994
[32] Kim SJ., et al., 1997
[33] Lawrence F., et al., 1974
[34] Monteilhet C., et al., 1974
[35] Old IG., et al., 1993
[36] Osumi M., et al., 1971
[37] Posorske LH., et al., 1979
[38] Robert-Gero M., et al., 1972
[39] Romby P., et al., 1992
[40] Schulman LH., et al., 1981
[41] Shepard A., et al., 1992
[42] Sikora M., et al., 2009
[43] Strom AM., et al., 2014
[44] Svensson I. 1967
[45] Svensson I. 1968
[46] Truong F., et al., 2012
[47] Urbanowski ML., et al., 1987
[48] Valenzuela D., et al., 1984
[49] Varshney U., et al., 1992
[50] Walker EJ., et al., 1988
[51] Waller J., et al., 1971
[52] Yamashiro-Matsumura S., et al., 1981
External database links:  
DIP:
DIP-10194N
ECOCYC:
METG-MONOMER
ECOLIWIKI:
b2114
INTERPRO:
IPR033911
INTERPRO:
IPR029038
INTERPRO:
IPR023458
INTERPRO:
IPR015413
INTERPRO:
IPR001412
INTERPRO:
IPR014729
INTERPRO:
IPR012340
INTERPRO:
IPR009080
INTERPRO:
IPR004495
INTERPRO:
IPR002547
INTERPRO:
IPR041872
INTERPRO:
IPR014758
MODBASE:
P00959
PDB:
3H99
PDB:
3H97
PDB:
3H9C
PDB:
3H9B
PDB:
1F4L
PDB:
1MEA
PDB:
1MED
PDB:
1P7P
PDB:
1PFU
PDB:
1PFV
PDB:
1PFW
PDB:
1PFY
PDB:
1PG0
PDB:
1PG2
PDB:
1QQT
PFAM:
PF09334
PFAM:
PF01588
PRIDE:
P00959
PRINTS:
PR01041
PRODB:
PRO_000023213
PROSITE:
PS00178
PROSITE:
PS50886
REFSEQ:
NP_416617
SMR:
P00959
SWISSMODEL:
P00959
UNIPROT:
P00959


Operon      
Name: metG         
Operon arrangement:
Transcription unit        Promoter
metG
metG


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter mrpp2 2194175 reverse Similarity to the consensus
Read more >
[ICWHO] [53]
  promoter mrpp7 2194180 reverse Similarity to the consensus
Read more >
[ICWHO] [53]
  promoter TSS_2438 2194185 reverse nd [RS-EPT-CBR] [54]
  promoter TSS_2439 (cluster) 2194194 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [54]
  promoter TSS_2440 (cluster) 2194200 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [54]
  promoter TSS_2441 2194222 reverse nd [RS-EPT-CBR] [54]


Evidence    

 [ICWHO] Inferred computationally without human oversight

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Abdeljabbar DM., Klein TJ., Zhang S., Link AJ., 2009, A single genomic copy of an engineered methionyl-tRNA synthetase enables robust incorporation of azidonorleucine into recombinant proteins in E. coli., J Am Chem Soc 131(47):17078-9

 [2] Armstrong JB., Fairfield JA., 1975, A new method for the isolation of methionyl transfer RNA synthetase mutants from Escherichia coli., Can J Microbiol 21(6):754-8

 [3] Barker DG., Ebel JP., Jakes R., Bruton CJ., 1982, Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment., Eur J Biochem 127(3):449-57

 [4] Berne PF., Schmitter JM., Blanquet S., 1990, Peptide and protein carboxyl-terminal labeling through carboxypeptidase Y-catalyzed transpeptidation., J Biol Chem 265(32):19551-9

 [5] Blanquet S., Dessen P., 1976, Antico-operative binding of bacterial and mammalian initiator tRNAMet to methionyl-tRNA synthetase from escherichia coli., J Mol Biol 103(4):765-84

 [6] Bruton C., Jakes R., Atkinson T., 1975, Gram-scale purification of methionyl-tRNA and tyrosyl-tRNA synthetases from Escherichia coli., Eur J Biochem 59(2):327-33

 [7] Bruton CJ., Hartley BS., 1970, Chemical studies on methionyl-tRNA synthetase from Escherichia coli., J Mol Biol 52(2):165-78

 [8] Bruton CJ., Jakes R., Koch GL., 1974, Repeated sequences in methionyl-tRNA synthetase from E. coli., FEBS Lett 45(1):26-8

 [9] Cassio D., 1968, [Study of methionyl tRNA synthetase of Escherichia coli. 2. Selective and reversible inactivation of the capacity to activate tRNA]., Eur J Biochem 4(2):222-4

 [10] Cassio D., Lawrence F., Lawrence DA., 1970, Level of methionyl-tRNA synthetase in merodiploids of Escherichia coli K12., Eur J Biochem 15(2):331-4

 [11] Cassio D., Waller J., 1971, Purification and properties of methionyl-tRNA synthetase from E. coli K 12 carrying the F32 episome., FEBS Lett 12(6):309-312

 [12] Cassio D., Waller JP., 1968, [Study of methionyl-tRNA synthetase from Escherichia coli. 3. Dissociation into active subunits by the action of an extrinsic factor]., Eur J Biochem 5(1):33-41

 [13] Cassio D., Waller JP., 1971, Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme., Eur J Biochem 20(2):283-300

 [14] Dardel F., Panvert M., Blanquet S., Fayat G., 1991, Locations of the metG and mrp genes on the physical map of Escherichia coli., J Bacteriol 173(11):3273

 [15] Dessen P., Fayat G., Zaccai G., Blanquet S., 1982, Neutron-scattering studies of the binding of initiator tRNAMet to escherichia coli trypsin modified methionyl-tRNA synthetase., J Mol Biol 154(4):603-13

 [16] Dessen P., Zaccai G., Blanquet S., 1985, Methionyl-tRNA synthetase from E. coli: direct evidence for exchange of protomers in the dimeric enzyme by using deuteration and small-angle neutron scattering., Biochimie 67(6):637-41

 [17] Dube SK., 1973, Evidence of "three point" attachment of tRNA to methionyl tRNA synthetase., Nat New Biol 243(125):103-5

 [18] Fayat G., Fromant M., Kahn D., Blanquet S., 1977, Affinity chromatography on agarose-hexyl-adenosine-5'-phosphate of methionyl-tRNA synthetase from Escherichia coli. Application of the couplings between the methionine and ATP sites., Eur J Biochem 78(2):333-6

 [19] Fayat G., Hountondji C., Blanquet S., 1979, Methionyl-tRNA synthetase from Escherichia coli. Inactivation and labeling by periodate-treated initiator tRNA., Eur J Biochem 96(1):87-92

 [20] Gillet S., Hountondji C., Schmitter JM., Blanquet S., 1997, Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry., Protein Sci 6(11):2426-35

 [21] Graffe M., Dondon J., Caillet J., Romby P., Ehresmann C., Ehresmann B., Springer M., 1992, The specificity of translational control switched with transfer RNA identity rules., Science 255(5047):994-6

 [22] Gulik A., Monteilhet C., Dessen P., Fayat G., 1976, Small-angle x-ray and light-scattering study of native and trypsin-modified methionyl-tRNA synthetase from Escherichia coli., Eur J Biochem 64(1):295-300

 [23] Hirel PH., Leveque F., Mellot P., Dardel F., Panvert M., Mechulam Y., Fayat G., 1988, Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase--beta-galactosidase chimeric protein., Biochimie 70(6):773-82

 [24] Hountondji C., Fayat G., Blanquet S., 1979, Complete inactivation and labeling of methionyl-tRNA synthetase by periodate-treated initiator tRNA in the presence of sodium cyanohydridoborate., Eur J Biochem 102(1):247-50

 [25] Hountondji C., Lederer F., Dessen P., Blanquet S., 1986, Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3'-end of tRNA., Biochemistry 25(1):16-21

 [26] Jakubowski H., 2000, Translational incorporation of S-nitrosohomocysteine into protein., J Biol Chem 275(29):21813-6

 [27] Jakubowski H., 2002, The determination of homocysteine-thiolactone in biological samples., Anal Biochem 308(1):112-9

 [28] Jakubowski H., 1993, Energy cost of proofreading in vivo: the charging of methionine tRNAs in Escherichia coli., FASEB J 7(1):168-72

 [29] Kabir MM., Shimizu K., 2001, Proteome analysis of a temperature-inducible recombinant Escherichia coli for poly-beta-hydroxybutyrate production., J Biosci Bioeng 92(3):277-84

 [30] Kalogerakos T., Blanquet S., Waller JP., 1979, Cobalt(III) labeling of methionyl-tRNA synthetase from Escherichia coli., Eur J Biochem 93(2):339-43

 [31] Kalogerakos T., Hountondji C., Berne PF., Dukta S., Blanquet S., 1994, Modification of aminoacyl-tRNA synthetases with pyridoxal-5'-phosphate. Identification of the labeled amino acid residues., Biochimie 76(1):33-44

 [32] Kim SJ., Kim S., 1997, Temperature sensitivity of a class I tRNA synthetase induced by artificial breakage of polypeptide chain., Mol Cells 7(3):389-93

 [33] Lawrence F., Shire DJ., Waller JP., 1974, The effect of adenosine analogues on the ATP-pyrophosphate exchange reaction catalysed by methionyl-tRNA synthetase., Eur J Biochem 41(1):73-81

 [34] Monteilhet C., Zelwer C., Risler JL., 1974, Two isomorphous heavy-atom derivatives of crystalline methionyl-tRNA synthetase from Escherichia coli., FEBS Lett 46(1):101-5

 [35] Old IG., Saint Girons I., Richaud C., 1993, Physical mapping of the scattered methionine genes on the Escherichia coli chromosome., J Bacteriol 175(11):3689-91

 [36] Osumi M., Imahori K., 1971, [Methionyl tRNA synthetase--interaction of enzymes and the substrate]., Tanpakushitsu Kakusan Koso 16(11):993-9

 [37] Posorske LH., Cohn M., Yanagisawa N., Auld DS., 1979, Methionyl-tRNA synthetase of Escherichia coli. A zinc metalloprotein., Biochim Biophys Acta 576(1):128-33

 [38] Robert-Gero M., Waller JP., 1972, Purification of methionyl-tRNA synthetase from Escherichia coli K12 by affinity chromatography., Eur J Biochem 31(2):315-9

 [39] Romby P., Brunel C., Caillet J., Springer M., Grunberg-Manago M., Westhof E., Ehresmann C., Ehresmann B., 1992, Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules., Nucleic Acids Res 20(21):5633-40

 [40] Schulman LH., Valenzuela D., Pelka H., 1981, Reversible inactivation of Escherichia coli methionyl-tRNA synthetase by covalent attachment of formylmethionine tRNA to the tRNA binding site with a cleavable cross-linker., Biochemistry 20(21):6018-23

 [41] Shepard A., Shiba K., Schimmel P., 1992, RNA binding determinant in some class I tRNA synthetases identified by alignment-guided mutagenesis., Proc Natl Acad Sci U S A 89(20):9964-8

 [42] Sikora M., Jakubowski H., 2009, Homocysteine editing and growth inhibition in Escherichia coli., Microbiology 155(Pt 6):1858-65

 [43] Strom AM., Fehling SC., Bhattacharyya S., Hati S., 2014, Probing the global and local dynamics of aminoacyl-tRNA synthetases using all-atom and coarse-grained simulations., J Mol Model 20(5):2245

 [44] Svensson I., 1967, Studies on methionyl-tRNA synthetase. II. Effects of divalent and monovalent cations on methionyl-tRNA synthetase from Escherichia coli., Biochim Biophys Acta 146(1):253-8

 [45] Svensson I., 1968, Studies on methionyl-tRNA synthetase. 3. Enzyme dependence for maximum methionyl-tRNA formation., Biochim Biophys Acta 167(1):179-83

 [46] Truong F., Yoo TH., Lampo TJ., Tirrell DA., 2012, Two-strain, cell-selective protein labeling in mixed bacterial cultures., J Am Chem Soc 134(20):8551-6

 [47] Urbanowski ML., Plamann LS., Stauffer GV., 1987, Mutations affecting the regulation of the metB gene of Salmonella typhimurium LT2., J Bacteriol 169(1):126-30

 [48] Valenzuela D., Leon O., Schulman LH., 1984, Modification of specific lysine residues in E. coli methionyl-tRNA synthetase by crosslinking to E. coli formylmethionine tRNA., Biochem Biophys Res Commun 119(2):677-84

 [49] Varshney U., RajBhandary UL., 1992, Role of methionine and formylation of initiator tRNA in initiation of protein synthesis in Escherichia coli., J Bacteriol 174(23):7819-26

 [50] Walker EJ., Jeffrey PD., 1988, Sequence comparisons in the aminoacyl-tRNA synthetases with emphasis on regions of likely homology with sequences in the Rossmann fold in the methionyl and tyrosyl enzymes., Protein Seq Data Anal 1(3):187-93

 [51] Waller J., Risler J., Monteilhet C., Zelwer C., 1971, Crystallisation of trypsin-modified methionyl-tRNA synthetase from Escherichia coli., FEBS Lett 16(3):186-188

 [52] Yamashiro-Matsumura S., Kawata M., 1981, Methionyl-tRNA synthetase-induced conformational change of Escherichia coli tRNAfMet., J Biol Chem 256(17):9308-12

 [53] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [54] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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