RegulonDB RegulonDB 10.8: Gene Form
   

rplT gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

rplT rpmI pheM Cis-reg; leader anti-terminator terminator anti-anti-terminator TSS_2016 TSS_2016 TSS_2015 TSS_2015 TSS_2014 (cluster) TSS_2014 (cluster) rplTp rplTp TSS_2013 TSS_2013 pheMp pheMp

Gene      
Name: rplT    Texpresso search in the literature
Synonym(s): ECK1714, EG10881, b1716, pdzA
Genome position(nucleotides): 1799393 <-- 1799749 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
48.18
External database links:  
ASAP:
ABE-0005729
CGSC:
17608
ECHOBASE:
EB0874
OU-MICROARRAY:
b1716
PortEco:
rplT
STRING:
511145.b1716
COLOMBOS: rplT


Product      
Name: 50S ribosomal subunit protein L20
Synonym(s): PdzA, RplT
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol,ribosome
Molecular weight: 13.497
Isoelectric point: 12.003
Motif(s):
 
Type Positions Sequence
3 -> 109 RVKRGVIARARHKKILKQAKGYYGARSRVYRVAFQAVIKAGQYAYRDRRQRKRQFRQLWIARINAAARQNGISYSKFINGLKKASVEIDRKILADIAVFDKVAFTAL
2 -> 118 ARVKRGVIARARHKKILKQAKGYYGARSRVYRVAFQAVIKAGQYAYRDRRQRKRQFRQLWIARINAAARQNGISYSKFINGLKKASVEIDRKILADIAVFDKVAFTALVEKAKAALA
33 -> 33 R

 

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
  3 - regulation --> 3.1 - type of regulation --> 3.1.3 - posttranscriptional
  6 - cell structure --> 6.6 - ribosomes
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0005840 - ribosome
GO:0022625 - cytosolic large ribosomal subunit
molecular_function GO:0000900 - translation repressor activity, mRNA regulatory element binding
GO:0003735 - structural constituent of ribosome
GO:0003723 - RNA binding
GO:0003729 - mRNA binding
GO:0019843 - rRNA binding
GO:0070180 - large ribosomal subunit rRNA binding
biological_process GO:0006412 - translation
GO:0000027 - ribosomal large subunit assembly
GO:0017148 - negative regulation of translation
Note(s): Note(s): ...[more].
Reference(s): [1] Agafonov DE., et al., 1997
[2] Barritault D., et al., 1975
[3] Bernabeu C., et al., 1979
[4] Brombach M., et al., 1987
[5] Fayat G., et al., 1983
[6] Fu Y., et al., 2013
[7] Gongadze GM., et al., 1986
[8] Hardy SJ. 1975
[9] Herold M., et al., 1987
[10] Huang SC., et al., 1990
[11] Kashiwagi K., et al., 1987
[12] Kazemie M. 1976
[13] Lee J., et al., 2006
[14] Lesage P., et al., 1992
[15] Lotti M., et al., 1989
[16] Mayaux JF., et al., 1983
[17] Morrison CA., et al., 1977
[18] Ramagopal S. 1984
[19] Rippa V., et al., 2010
[20] Rohl R., et al., 1982
[21] Shen V., et al., 1980
[22] Skold SE. 1981
[23] Springer M., et al., 1985
[24] Sumpter VG., et al., 1991
[25] Wertheimer SJ., et al., 1988
[26] Willumeit R., et al., 2001
[27] Wittmann-Liebold B., et al., 1979
[28] Yusupov MM., et al., 1986
External database links:  
DIP:
DIP-47941N
ECOCYC:
EG10881-MONOMER
ECOLIWIKI:
b1716
INTERPRO:
IPR035566
INTERPRO:
IPR005813
MINT:
MINT-1321645
MODBASE:
P0A7L3
PANTHER:
PTHR10986
PDB:
2J28
PDB:
2RDO
PDB:
3BBX
PDB:
3J5L
PDB:
3J7Z
PDB:
3J8G
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:
6GC4
PDB:
6GC6
PDB:
6GC7
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:
PF00453
PRIDE:
P0A7L3
PRINTS:
PR00062
PRODB:
PRO_000023826
PROSITE:
PS00937
REFSEQ:
NP_416231
SMR:
P0A7L3
UNIPROT:
P0A7L3


Operon      
Name: thrS-infC-rpmI-rplT-pheMST-ihfA         
Operon arrangement:
Transcription unit        Promoter
ihfA
pheM
pheMST-ihfA
rplT
rplT-pheM
rpmI-rplT
infC-rpmI-rplT
infC
thrS-infC
thrS-infC-rpmI-rplT-pheMST-ihfA


Transcriptional Regulation      
Display Regulation             
Repressed by: NsrR, FNR


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 TSS_2013 1799621 reverse nd [RS-EPT-CBR] [29]
  promoter TSS_2014 (cluster) 1799992 reverse For this promoter, there
Read more >
[RS-EPT-CBR] [29]
  promoter TSS_2015 1799997 reverse nd [RS-EPT-CBR] [29]
  promoter TSS_2016 1799999 reverse nd [RS-EPT-CBR] [29]


Evidence    

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



Reference(s)    

 [1] Agafonov DE., Kolb VA., Spirin AS., 1997, Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique., Proc Natl Acad Sci U S A 94(24):12892-7

 [2] Barritault D., Expert-Bezancon A., Milet M., 1975, [Nearest-neighbor relationships among 50S ribosomal proteins of E. coli]., C R Acad Sci Hebd Seances Acad Sci D 281(14):1043-6

 [3] Bernabeu C., Vazquez D., Conde FP., 1979, Comparative study between prokaryotes and eukaryotes by chemical iodination of ribosomal proteins., Biochim Biophys Acta 577(2):400-9

 [4] Brombach M., Pon CL., 1987, The unusual translational initiation codon AUU limits the expression of the infC (initiation factor IF3) gene of Escherichia coli., Mol Gen Genet 208(1-2):94-100

 [5] Fayat G., Mayaux JF., Sacerdot C., Fromant M., Springer M., Grunberg-Manago M., Blanquet S., 1983, Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20., J Mol Biol 171(3):239-61

 [6] Fu Y., Deiorio-Haggar K., Anthony J., Meyer MM., 2013, Most RNAs regulating ribosomal protein biosynthesis in Escherichia coli are narrowly distributed to Gammaproteobacteria., Nucleic Acids Res 41(6):3491-503

 [7] Gongadze GM., Selivanova OM., Gudkov AT., Vasiliev VD., 1986, Structure of protein-deficient 50 S ribosomal subunits. Nine core proteins induce the compact conformation of 23 S ribosomal RNA., FEBS Lett 197(1-2):74-8

 [8] Hardy SJ., 1975, The stoichiometry of the ribosomal proteins of Escherichia coli., Mol Gen Genet 140(3):253-74

 [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] Huang SC., Panagiotidis CA., Canellakis ES., 1990, Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli., Proc Natl Acad Sci U S A 87(9):3464-8

 [11] Kashiwagi K., Igarashi K., 1987, Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity., Biochim Biophys Acta 911(2):180-90

 [12] Kazemie M., 1976, Binding of aminoacyl-tRNA to reconstituted subparticles of Escherichia coli large ribosomal subunits., Eur J Biochem 67(2):373-8

 [13] Lee J., Cao L., Ow SY., Barrios-Llerena ME., Chen W., Wood TK., Wright PC., 2006, Proteome changes after metabolic engineering to enhance aerobic mineralization of cis-1,2-dichloroethylene., J Proteome Res 5(6):1388-97

 [14] Lesage P., Chiaruttini C., Graffe M., Dondon J., Milet M., Springer M., 1992, Messenger RNA secondary structure and translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and the ribosomal proteins, L35 and L20., J Mol Biol 228(2):366-86

 [15] Lotti M., Noah M., Stoffler-Meilicke M., Stoffler G., 1989, Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy., Mol Gen Genet 216(2-3):245-53

 [16] Mayaux JF., Fayat G., Fromant M., Springer M., Grunberg-Manago M., Blanquet S., 1983, Structural and transcriptional evidence for related thrS and infC expression., Proc Natl Acad Sci U S A 80(20):6152-6

 [17] Morrison CA., Tischendorf G., Stoffler G., Garrett RA., 1977, Accessibility of proteins in 50S ribosomal subunits of Escherichia coli to antibodies: an ultracentrifugation study., Mol Gen Genet 151(3):245-52

 [18] Ramagopal S., 1984, Metabolic changes in ribosomes of Escherichia coli during prolonged culture in different media., Eur J Biochem 140(2):353-61

 [19] Rippa V., Cirulli C., Di Palo B., Doti N., Amoresano A., Duilio A., 2010, The ribosomal protein L2 interacts with the RNA polymerase alpha subunit and acts as a transcription modulator in Escherichia coli., J Bacteriol 192(7):1882-9

 [20] Rohl R., Nierhaus KH., 1982, Assembly map of the large subunit (50S) of Escherichia coli ribosomes., Proc Natl Acad Sci U S A 79(3):729-33

 [21] Shen V., King TC., Kumar V., Daugherty B., 1980, Monoclonal antibodies to Escherichia coli 50S ribosomes., Nucleic Acids Res 8(20):4639-49

 [22] Skold SE., 1981, RNA-protein complexes identified by crosslinking of polysomes., Biochimie 63(1):53-60

 [23] Springer M., Mayaux JF., Fayat G., Plumbridge JA., Graffe M., Blanquet S., Grunberg-Manago M., 1985, Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon., J Mol Biol 181(4):467-78

 [24] Sumpter VG., Tate WP., Nowotny P., Nierhaus KH., 1991, Modification of histidine residues on proteins from the 50S subunit of the Escherichia coli ribosome. Effects on subunit assembly and peptidyl transferase centre activity., Eur J Biochem 196(2):255-60

 [25] Wertheimer SJ., Klotsky RA., Schwartz I., 1988, Transcriptional patterns for the thrS-infC-rplT operon of Escherichia coli., Gene 63(2):309-20

 [26] Willumeit R., Diedrich G., Forthmann S., Beckmann J., May RP., Stuhrmann HB., Nierhaus KH., 2001, Mapping proteins of the 50S subunit from Escherichia coli ribosomes., Biochim Biophys Acta 1520(1):7-20

 [27] Wittmann-Liebold B., Seib C., 1979, The primary structure of protein L20 from the large subunit of the Escherichia coli ribosome., FEBS Lett 103(1):61-5

 [28] Yusupov MM., Spirin AS., 1986, Are there proteins between the ribosomal subunits? Hot tritium bombardment experiments., FEBS Lett 197(1-2):229-33

 [29] 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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