RegulonDB RegulonDB 10.10: Gene Form
   

rplX gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

rplE rplN rplX TSS_3774 (cluster) TSS_3774 (cluster) TSS_3773 TSS_3773 TSS_3772 TSS_3772 TSS_3771 (cluster) TSS_3771 (cluster) TSS_3770 TSS_3770 TSS_3769 TSS_3769 TSS_3768 (cluster) TSS_3768 (cluster) TSS_3767 (cluster) TSS_3767 (cluster)

Gene      
Name: rplX    Texpresso search in the literature
Synonym(s): ECK3296, EG10884, b3309
Genome position(nucleotides): 3447453 <-- 3447767 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
46.03
External database links:  
ASAP:
ABE-0010835
CGSC:
243
ECHOBASE:
EB0877
ECOLIHUB:
rplX
OU-MICROARRAY:
b3309
STRING:
511145.b3309
COLOMBOS: rplX


Product      
Name: 50S ribosomal subunit protein L24
Synonym(s): RplX
Sequence: Get amino acid sequence Fasta Format
Cellular location: ribosome,cytosol
Molecular weight: 11.316
Isoelectric point: 11.008
Motif(s):
 
Type Positions Sequence
8 -> 37 DDEVIVLTGKDKGKRGKVKNVLSSGKVIVE
39 -> 103 INLVKKHQKPVPALNQPGGIVEKEAAIQVSNVAIFNAATGKADRVGFRFEDGKKVRFFKSNSETI
2 -> 104 AAKIRRDDEVIVLTGKDKGKRGKVKNVLSSGKVIVEGINLVKKHQKPVPALNQPGGIVEKEAAIQVSNVAIFNAATGKADRVGFRFEDGKKVRFFKSNSETIK

 

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:0022625 - cytosolic large ribosomal subunit
molecular_function GO:0003735 - structural constituent of ribosome
GO:0005515 - protein binding
GO:0003723 - RNA binding
GO:0019843 - rRNA binding
GO:0070180 - large ribosomal subunit rRNA binding
biological_process GO:0006412 - translation
GO:0000027 - ribosomal large subunit assembly
Note(s): Note(s): ...[more].
Reference(s): [1] Agafonov DE., et al., 1997
[2] Bausk EV., et al., 1985
[3] Cabezon T., et al., 1977
[4] Cerretti DP., et al., 1983
[5] Dabbs ER., et al., 1983
[6] Fallon AM., et al., 1979
[7] Giocanti N., et al., 1980
[8] Giri L., et al., 1979
[9] Graifer DM., et al., 1989
[10] Hernandez F., et al., 1977
[11] Herold M., et al., 1987
[12] Isono K., et al., 1976
[13] Iusupov MM., et al., 1986
[14] Jaskunas SR., et al., 1977
[15] Kakegawa T., et al., 1986
[16] Kazemie M. 1976
[17] Kudva R., et al., 2018
[18] Leffers H., et al., 1988
[19] Liang ST., et al., 1999
[20] Menetret JF., et al., 2007
[21] Oste C., et al., 1977
[22] Ostergaard P., et al., 1998
[23] Parfait R., et al., 1976
[24] Skinner RH., et al., 1985
[25] Sloof P., et al., 1976
[26] Sloof P., et al., 1978
[27] Tumanova LG., et al., 1984
[28] Tumanova LG., et al., 1983
[29] Vladimirov SN., et al., 1985
[30] Willumeit R., et al., 2001
[31] Wittmann-Liebold B. 1979
[32] Yates JL., et al., 1980
[33] Yusupov MM., et al., 1986
External database links:  
DIP:
DIP-47846N
ECOCYC:
EG10884-MONOMER
ECOLIWIKI:
b3309
INTERPRO:
IPR005824
INTERPRO:
IPR003256
INTERPRO:
IPR005825
INTERPRO:
IPR041988
INTERPRO:
IPR008991
INTERPRO:
IPR014722
MODBASE:
P60624
PANTHER:
PTHR12903
PDB:
1ML5
PDB:
2J28
PDB:
2RDO
PDB:
2VRH
PDB:
3BBX
PDB:
3J45
PDB:
3J46
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:
6DNC
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:
6O9J
PDB:
6O9K
PDB:
6OFX
PDB:
6OG7
PDB:
6ORE
PDB:
6ORL
PDB:
6OST
PDB:
6OT3
PDB:
6OUO
PDB:
6Q97
PDB:
6Q98
PDB:
6Q9A
PDB:
6QUL
PDB:
6S0K
PDB:
6SZS
PDB:
6TBV
PDB:
6TC3
PFAM:
PF17136
PFAM:
PF00467
PRIDE:
P60624
PRODB:
PRO_000023830
PROSITE:
PS01108
REFSEQ:
NP_417768
SMART:
SM00739
SMR:
P60624
UNIPROT:
P60624


Operon      
Name: rplNXE-rpsNH-rplFR-rpsE-rpmD-rplO-secY-rpmJ         
Operon arrangement:
Transcription unit        Promoter
rplNXE-rpsNH-rplFR-rpsE-rpmD-rplO-secY-rpmJ


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_3767 (cluster) 3447230 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3768 (cluster) 3447242 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3769 3447245 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3770 3447267 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3771 (cluster) 3447453 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3772 3447455 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3773 3447457 reverse nd [RS-EPT-CBR] [34]
  promoter TSS_3774 (cluster) 3447461 reverse nd [RS-EPT-CBR] [34]


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] Bausk EV., Graifer DM., Karpova GG., 1985, [Study of the photoaffinity modification of Escherichia coli ribosomes near the donor tRNA-binding center]., Mol Biol (Mosk) 19(2):545-52

 [3] Cabezon T., Herzog A., Petre J., Yaguchi M., Bollen A., 1977, Ribosomal assembly deficiency in an Escherichia coli thermosensitive mutant having an altered L24 ribosomal protein., J Mol Biol 116(3):361-74

 [4] Cerretti DP., Dean D., Davis GR., Bedwell DM., Nomura M., 1983, The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene., Nucleic Acids Res 11(9):2599-616

 [5] 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

 [6] Fallon AM., Jinks CS., Yamamoto M., Nomura M., 1979, Expression of ribosomal protein genes cloned in a hybrid plasmid in Escherichia coli: gene dosage effects on synthesis of ribosomal proteins and ribosomal protein messenger ribonucleic acid., J Bacteriol 138(2):383-96

 [7] Giocanti N., Ekert B., 1980, Radiochemical cross-linking of proteins to RNA within ribosomal subunits from E. colil MRE 600., Int J Radiat Biol Relat Stud Phys Chem Med 38(1):63-82

 [8] Giri L., Dijk J., 1979, Physical studies on proteins L3 and L24 from the 50 S subunit of the Escherichia coli ribosome., Arch Biochem Biophys 193(1):122-9

 [9] Graifer DM., Babkina GT., Matasova NB., Vladimirov SN., Karpova GG., Vlassov VV., 1989, Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives., Biochim Biophys Acta 1008(2):146-56

 [10] Hernandez F., Vazquez D., Ballesta JP., 1977, Functional roles of 50-S ribosomal proteins., Eur J Biochem 78(1):267-72

 [11] 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

 [12] Isono K., Krauss J., Hirota Y., 1976, Isolation and characterization of temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins., Mol Gen Genet 149(3):297-302

 [13] Iusupov MM., Spirin AS., 1986, [Study of the surface of Escherichia coli ribosomes and ribosomal particles by the tritium bombardment method]., Biokhimiia 51(11):1858-67

 [14] Jaskunas SR., Fallon AM., Nomura M., 1977, Identification and organization of ribosomal protein genes of Escherichia coli carried by lambdafus2 transducing phage., J Biol Chem 252(20):7323-36

 [15] Kakegawa T., Sato E., Hirose S., Igarashi K., 1986, Polyamine binding sites on Escherichia coli ribosomes., Arch Biochem Biophys 251(2):413-20

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

 [17] Kudva R., Tian P., Pardo-Avila F., Carroni M., Best RB., Bernstein HD., von Heijne G., 2018, The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding., Elife 7

 [18] Leffers H., Egebjerg J., Andersen A., Christensen T., Garrett RA., 1988, Domain VI of Escherichia coli 23 S ribosomal RNA. Structure, assembly and function., J Mol Biol 204(3):507-22

 [19] Liang ST., Ehrenberg M., Dennis P., Bremer H., 1999, Decay of rplN and lacZ mRNA in Escherichia coli., J Mol Biol 288(4):521-38

 [20] Menetret JF., Schaletzky J., Clemons WM., Osborne AR., Skanland SS., Denison C., Gygi SP., Kirkpatrick DS., Park E., Ludtke SJ., Rapoport TA., Akey CW., 2007, Ribosome binding of a single copy of the SecY complex: implications for protein translocation., Mol Cell 28(6):1083-92

 [21] Oste C., Parfait R., Bollen A., Crichton RR., 1977, A new nucleic acid-protein cross-linking reagent., Mol Gen Genet 152(3):253-7

 [22] Ostergaard P., Phan H., Johansen LB., Egebjerg J., Ostergaard L., Porse BT., Garrett RA., 1998, Assembly of proteins and 5 S rRNA to transcripts of the major structural domains of 23 S rRNA., J Mol Biol 284(2):227-40

 [23] Parfait R., De Wolf B., Crichton RR., 1976, Protein-RNA interactions in the Escherichia coli ribosome: L24 protein-23 S RNA complex., Arch Int Physiol Biochim 84(2):404-5

 [24] Skinner RH., Stark MJ., Dahlberg AE., 1985, Mutations within the 23S rRNA coding sequence of E. coli which block ribosome assembly., EMBO J 4(6):1605-8

 [25] Sloof P., Garrett RA., Nanninga N., 1976, An investigation of the binding sites of proteins S8, L23 and L24 on the ribosomal RNAs of Escherichia coli by electron microscopy., Mol Gen Genet 147(2):129-38

 [26] Sloof P., Hunter JB., Garrett RA., Branlant C., 1978, RNA-RNA interactions in the binding site of protein L24 on 23S ribosomal RNA of Escherichia coli: 1. Evidence for their occurrence between widely separated sequence regions., Nucleic Acids Res 5(10):3503-13

 [27] Tumanova LG., Gongadze GM., Ven'iaminov SIu., Gudkov AT., Bushuev VN., 1984, [Comparison of the physical properties of ribosomal proteins from Escherichia coli 50S subparticles isolated by different methods]., Mol Biol (Mosk) 18(3):751-8

 [28] Tumanova LG., Gongadze GM., Venyaminov SYu., Gudkov AT., Bushuev VN., 1983, Physical properties of ribosomal proteins isolated under different conditions from the Escherichia coli 50 S subunit., FEBS Lett 157(1):85-90

 [29] Vladimirov SN., Graifer DM., Karpova GG., Semenkov YuP., Makhno VI., Kirillov SV., 1985, The effect of GTP hydrolysis and transpeptidation on the arrangement of aminoacyl-tRNA at the A-site of Escherichia coli 70 S ribosomes., FEBS Lett 181(2):367-72

 [30] 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

 [31] Wittmann-Liebold B., 1979, Primary structure of protein L24 from the Escherichia coli ribosome., FEBS Lett 108(1):75-80

 [32] Yates JL., Arfsten AE., Nomura M., 1980, In vitro expression of Escherichia coli ribosomal protein genes: autogenous inhibition of translation., Proc Natl Acad Sci U S A 77(4):1837-41

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

 [34] 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.


RegulonDB