RegulonDB RegulonDB 10.8: Gene Form
   

rpmG gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

Gene      
Name: rpmG    Texpresso search in the literature
Synonym(s): ECK3626, EG10891, b3636
Genome position(nucleotides): 3811250 <-- 3811417 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
40.48
External database links:  
ASAP:
ABE-0011883
CGSC:
236
ECHOBASE:
EB0884
OU-MICROARRAY:
b3636
PortEco:
rpmG
STRING:
511145.b3636
COLOMBOS: rpmG


Product      
Name: 50S ribosomal subunit protein L33
Synonym(s): RpmG
Sequence: Get amino acid sequence Fasta Format
Cellular location: ribosome,cytosol
Molecular weight: 6.372
Isoelectric point: 10.965
Motif(s):
 
Type Positions Sequence
2 -> 55 AKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK
7 -> 53 EKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAK
48 -> 49 IY

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.2 - translation
  2 - information transfer --> 2.3 - protein related --> 2.3.8 - ribosomal proteins
  6 - cell structure --> 6.6 - ribosomes
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0005840 - ribosome
GO:0015934 - large ribosomal subunit
GO:0022625 - cytosolic large ribosomal subunit
molecular_function GO:0003735 - structural constituent of ribosome
GO:0003723 - RNA binding
GO:0000049 - tRNA binding
biological_process GO:0006412 - translation
GO:0000027 - ribosomal large subunit assembly
GO:0046677 - response to antibiotic
Note(s): Note(s): ...[more].
Reference(s): [1] Butler PD., et al., 1985
[2] Butler PD., et al., 1984
[3] Chang CN., et al., 1975
[4] Chang CN., et al., 1976
[5] Chang FN., et al., 1974
[6] Dabbs ER., et al., 1983
[7] Dzionara M., et al., 1977
[8] Gimautdinova OI., et al., 1984
[9] Herold M., et al., 1987
[10] Isono K., et al., 1977
[11] Isono K., et al., 1980
[12] Kirillov SV., et al., 1999
[13] Kitakawa M., et al., 1980
[14] Korepanov AP., et al., 2012
[15] Laughrea M., et al., 1987
[16] Lee JS., et al., 1981
[17] Markey F., et al., 1976
[18] Matspalu E., et al., 1982
[19] Naaktgeboren N., et al., 1976
[20] Romero DP., et al., 1990
[21] Sander G., et al., 1975
[22] Ven'iaminova AG., et al., 1988
[23] Wower J., et al., 1994
[24] van de Ven FJ., et al., 1983
External database links:  
DIP:
DIP-35968N
DISPROT:
DP00143
ECOCYC:
EG10891-MONOMER
ECOLIWIKI:
b3636
INTERPRO:
IPR001705
INTERPRO:
IPR038584
INTERPRO:
IPR011332
INTERPRO:
IPR018264
MINT:
MINT-1234559
MODBASE:
P0A7N9
PDB:
2J28
PDB:
2RDO
PDB:
3BBX
PDB:
3J5L
PDB:
3J5S
PDB:
3J7Z
PDB:
3J9Y
PDB:
3J9Z
PDB:
3JA1
PDB:
3JBU
PDB:
3JBV
PDB:
3JCD
PDB:
3JCE
PDB:
3JCJ
PDB:
3JCN
PDB:
4CSU
PDB:
4U1U
PDB:
4U1V
PDB:
4U20
PDB:
4U24
PDB:
4U25
PDB:
4U26
PDB:
4U27
PDB:
4UY8
PDB:
4V47
PDB:
4V48
PDB:
4V4H
PDB:
4V4Q
PDB:
4V4V
PDB:
4V4W
PDB:
4V50
PDB:
4V52
PDB:
4V53
PDB:
4V54
PDB:
4V55
PDB:
4V56
PDB:
4V57
PDB:
4V5B
PDB:
4V5H
PDB:
4V5Y
PDB:
4V64
PDB:
4V65
PDB:
4V66
PDB:
4V69
PDB:
4V6C
PDB:
4V6D
PDB:
4V6E
PDB:
4V6K
PDB:
4V6L
PDB:
4V6M
PDB:
4V6N
PDB:
4V6O
PDB:
4V6P
PDB:
4V6Q
PDB:
4V6R
PDB:
4V6S
PDB:
4V6T
PDB:
4V6V
PDB:
4V6Y
PDB:
4V6Z
PDB:
4V70
PDB:
4V71
PDB:
4V72
PDB:
4V73
PDB:
4V74
PDB:
4V75
PDB:
4V76
PDB:
4V77
PDB:
4V78
PDB:
4V79
PDB:
4V7A
PDB:
4V7B
PDB:
4V7C
PDB:
4V7D
PDB:
4V7I
PDB:
4V7S
PDB:
4V7T
PDB:
4V7U
PDB:
4V7V
PDB:
4V85
PDB:
4V89
PDB:
4V9C
PDB:
4V9D
PDB:
4V9O
PDB:
4V9P
PDB:
4WF1
PDB:
4WOI
PDB:
4WWW
PDB:
4YBB
PDB:
5ADY
PDB:
5AFI
PDB:
5AKA
PDB:
5GAD
PDB:
5GAE
PDB:
5GAF
PDB:
5GAG
PDB:
5GAH
PDB:
5H5U
PDB:
5IQR
PDB:
5IT8
PDB:
5J5B
PDB:
5J7L
PDB:
5J88
PDB:
5J8A
PDB:
5J91
PDB:
5JC9
PDB:
5JTE
PDB:
5JU8
PDB:
5KCR
PDB:
5KCS
PDB:
5KPS
PDB:
5KPV
PDB:
5KPW
PDB:
5KPX
PDB:
5L3P
PDB:
5LZA
PDB:
5LZB
PDB:
5LZC
PDB:
5LZD
PDB:
5LZE
PDB:
5LZF
PDB:
5MDV
PDB:
5MDW
PDB:
5MDY
PDB:
5MDZ
PDB:
5MGP
PDB:
5NCO
PDB:
5NP6
PDB:
5NWY
PDB:
5O2R
PDB:
5U4I
PDB:
5U9F
PDB:
5U9G
PDB:
5UYK
PDB:
5UYL
PDB:
5UYM
PDB:
5UYN
PDB:
5UYP
PDB:
5UYQ
PDB:
5WDT
PDB:
5WE4
PDB:
5WE6
PDB:
5WFK
PDB:
6BU8
PDB:
6BY1
PDB:
6C4I
PDB:
6ENF
PDB:
6ENJ
PDB:
6ENU
PDB:
6GBZ
PDB:
6GC0
PDB:
6GC8
PDB:
6GWT
PDB:
6GXM
PDB:
6GXN
PDB:
6GXO
PDB:
6GXP
PDB:
6H4N
PDB:
6H58
PDB:
6HRM
PDB:
6I0Y
PDB:
6I7V
PDB:
6OFX
PDB:
6OG7
PDB:
6Q97
PDB:
6Q98
PDB:
6Q9A
PDB:
6QUL
PFAM:
PF00471
PRIDE:
P0A7N9
PRODB:
PRO_000023839
PROSITE:
PS00582
REFSEQ:
NP_418093
SMR:
P0A7N9
UNIPROT:
P0A7N9


Operon      
Name: yicR-rpmBG-mutM         
Operon arrangement:
Transcription unit        Promoter
mutM
rpmBG
rpmBG-mutM
yicR-rpmBG
yicR-rpmBG-mutM
mutM


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 mutMp2 3811277 reverse The σ factor was determined
Read more >
[AIPP] [25]


Reference(s)    

 [1] Butler PD., Wild DG., 1985, The location of a mutation affecting ribosomal protein synthesis by Escherichia coli., J Gen Microbiol 131(1):135-44

 [2] Butler PD., Wild DG., 1984, Ribosomal protein synthesis by a mutant of Escherichia coli., Eur J Biochem 144(3):649-54

 [3] Chang CN., Chang N., 1975, Methylation of the ribosomal proteins in Escherichia coli. Nature and stoichiometry of the methylated amino acids in 50S ribosomal proteins., Biochemistry 14(3):468-77

 [4] Chang CN., Schwartz M., Chang FN., 1976, Identification and characterization of a new methylated amino acid in ribosomal protein L33 of Escherichia coli., Biochem Biophys Res Commun 73(2):233-9

 [5] Chang FN., Chang CN., Paik WK., 1974, Methylation of ribosomal proteins in Escherichia coli., J Bacteriol 120(2):651-6

 [6] Dabbs ER., Hasenbank R., Kastner B., Rak KH., Wartusch B., Stoffler G., 1983, Immunological studies of Escherichia coli mutants lacking one or two ribosomal proteins., Mol Gen Genet 192(3):301-8

 [7] Dzionara M., Robinson SM., Wittmann-Liebold B., 1977, Prediction for secondary structures of ten proteins from the 50S subunit of the Escherichia coli ribosome., J Supramol Struct 7(2):191-204

 [8] Gimautdinova OI., Zenkova MA., Karpova GG., Podust LM., 1984, [Affinity modification of Escherichia coli ribosomes with photoactivated analogs of mRNA]., Mol Biol (Mosk) 18(4):907-18

 [9] Herold M., Nierhaus KH., 1987, Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes., J Biol Chem 262(18):8826-33

 [10] Isono K., Cumberlidge AG., Isono S., 1977, Further temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins., Mol Gen Genet 152(3):239-43

 [11] Isono K., Schnier J., Kitakawa M., 1980, Genetic fine structure of the pyrE region containing the genes for ribosomal proteins L28 and L33 in Escherichia coli., Mol Gen Genet 179(2):311-7

 [12] Kirillov SV., Porse BT., Garrett RA., 1999, Peptidyl transferase antibiotics perturb the relative positioning of the 3'-terminal adenosine of P/P'-site-bound tRNA and 23S rRNA in the ribosome., RNA 5(8):1003-13

 [13] Kitakawa M., Blumenthal L., Isono K., 1980, Isolation and characterization of specialized transducing lambda phages carrying ribosomal protein genes of Escherichia coli., Mol Gen Genet 180(2):343-9

 [14] Korepanov AP., Korobeinikova AV., Shestakov SA., Garber MB., Gongadze GM., 2012, Protein L5 is crucial for in vivo assembly of the bacterial 50S ribosomal subunit central protuberance., Nucleic Acids Res 40(18):9153-9

 [15] Laughrea M., Latulippe J., Filion AM., Boulet L., 1987, Mistranslation in twelve Escherichia coli ribosomal proteins. Cysteine misincorporation at neutral amino acid residues other than tryptophan., Eur J Biochem 169(1):59-64

 [16] Lee JS., An G., Friesen JD., Isono K., 1981, Cloning and the nucleotide sequence of the genes for Escherichia coli ribosomal proteins L28 (rpmB) and L33 (rpmG)., Mol Gen Genet 184(2):218-23

 [17] Markey F., Sims PF., Wild DG., 1976, The composition of an unusual precursor of 50 S ribosomes in a mutant of Escherichia coli., Biochem J 158(2):451-6

 [18] Matspalu E., Ustav M., Villems R., 1982, The properties of the tRNA . protein complex of the Escherichia coli ribosome. Interaction with tRNA, 5-S RNA and 30-S ribosomal subunit., Eur J Biochem 124(2):269-73

 [19] Naaktgeboren N., Schrier P., Moller W., Voorma HO., 1976, The involvement of protein L11 in the joining of the 30-S initiation complex to the 50-S subunit., Eur J Biochem 62(1):117-23

 [20] Romero DP., Arredondo JA., Traut RR., 1990, Identification of a region of Escherichia coli ribosomal protein L2 required for the assembly of L16 into the 50 S ribosomal subunit., J Biol Chem 265(30):18185-91

 [21] Sander G., Marsh RC., Voigt J., Parmeggiani A., 1975, A comparative study of the 50S ribosomal subunit and several 50S subparticles in EF-T-and EF-G-dependent activities., Biochemistry 14(9):1805-14

 [22] Ven'iaminova AG., Vladimirov SN., Drygl SA., Zenkova MA., Karpova GG., 1988, [Affinity modification of Escherichia coli ribosomes with 2',3'-O-[4-(N-2-chloroethyl)-N-methylamino]-benzylidene derivative of AUGU3 in the 70S initiation complexes]., Bioorg Khim 14(3):321-32

 [23] Wower J., Hixson SS., Sylvers LA., Xing Y., Zimmermann RA., 1994, Synthesis of 2,6-diazido-9-(beta-D-ribofuranosyl)purine 3',5'-bisphosphate: incorporation into transfer RNA and photochemical labeling of Escherichia coli ribosomes., Bioconjug Chem 5(2):158-61

 [24] van de Ven FJ., de Bruin SH., Hilbers CW., 1983, 500-MHz 1H-NMR studies of ribosomal proteins isolated from 70-S ribosomes of Escherichia coli., Eur J Biochem 134(3):429-38

 [25] Zhao K., Liu M., Burgess RR., 2005, The global transcriptional response of Escherichia coli to induced sigma 32 protein involves sigma 32 regulon activation followed by inactivation and degradation of sigma 32 in vivo., J Biol Chem 280(18):17758-68


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