RegulonDB RegulonDB 10.10: Gene Form
   

htpG gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

htpG recR nc2 AscG terminator anti-terminator anti-anti-terminator adkp adkp TSS_641 TSS_641 TSS_640 TSS_640 htpGp2 htpGp2 TSS_639 TSS_639 TSS_638 TSS_638 htpGp1 htpGp1 htpGp3 htpGp3

Gene      
Name: htpG    Texpresso search in the literature
Synonym(s): ECK0467, EG10461, b0473
Genome position(nucleotides): 495120 --> 496994 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 52.85
External database links:  
ASAP:
 ABE-0001642
CGSC:
 17680
ECHOBASE:
 EB0456
ECOLIHUB:
 htpG
OU-MICROARRAY:
 b0473
STRING:
 511145.b0473
COLOMBOS: htpG


Product      
Name: chaperone protein HtpG
Synonym(s): C62.5, Hsp90, HtpG, heat shock protein 90
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol,inner membrane
Molecular weight: 71.422
Isoelectric point: 4.851
Motif(s):
 
Type Positions Sequence
554 -> 554 F
211 -> 622 EKREEKDGETVISWEKINKAQALWTRNKSEITDEEYKEFYKHIAHDFNDPLTWSHNRVEGKQEYTSLLYIPSQAPWDMWNRDHKHGLKLYVQRVFIMDDAEQFMPNYLRFVRGLIDSSDLPLNVSREILQDSTVTRNLRNALTKRVLQMLEKLAKDDAEKYQTFWQQFGLVLKEGPAEDFANQEAIAKLLRFASTHTDSSAQTVSLEDYVSRMKEGQEKIYYITADSYAAAKSSPHLELLRKKGIEVLLLSDRIDEWMMNYLTEFDGKPFQSVSKVDESLEKLADEVDESAKEAEKALTPFIDRVKALLGERVKDVRLTHRLTDTPAIVSTDADEMSTQMAKLFAAAGQKVPEVKYIFELNPDHVLVKRAADTEDEAKFSEWVELLLDQALLAERGTLEDPNLFIRRMNQLL
553 -> 624 LFAAAGQKVPEVKYIFELNPDHVLVKRAADTEDEAKFSEWVELLLDQALLAERGTLEDPNLFIRRMNQLLVS
550 -> 550 M
574 -> 574 H

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
GO:0016020 - membrane
GO:0005886 - plasma membrane
molecular_function GO:0005515 - protein binding
GO:0016887 - ATP hydrolysis activity
GO:0051082 - unfolded protein binding
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0042802 - identical protein binding
GO:0042803 - protein homodimerization activity
GO:0051087 - chaperone binding
GO:0044183 - protein folding chaperone
biological_process GO:0061992 - ATP-dependent chaperone mediated protein folding
GO:0006457 - protein folding
GO:0006974 - cellular response to DNA damage stimulus
GO:0009408 - response to heat
GO:0043093 - FtsZ-dependent cytokinesis
Note(s): Note(s): ...[more].
Reference(s): [1] Bolon DN. 2012
[2] Buchner J. 2010
[3] Doyle SM., et al., 2019
[4] Fauvet B., et al., 2021
[5] Pederson K., et al., 2017
[6] Shirai Y., et al., 1996
[7] Street TO., et al., 2012
[8] Ueguchi C., et al., 1992
External database links:  
DIP:
 DIP-29797N
ECOCYC:
 EG10461-MONOMER
ECOLIWIKI:
 b0473
INTERPRO:
 IPR020575
INTERPRO:
 IPR037196
INTERPRO:
 IPR036890
INTERPRO:
 IPR020568
INTERPRO:
 IPR019805
INTERPRO:
 IPR003594
INTERPRO:
 IPR001404
MODBASE:
 P0A6Z3
PANTHER:
 PTHR11528
PDB:
 1Y4S
PDB:
 2GQ0
PDB:
 2IOQ
PDB:
 2IOR
PDB:
 1SF8
PDB:
 1Y4U
PDB:
 2IOP
PFAM:
 PF00183
PFAM:
 PF02518
PRIDE:
 P0A6Z3
PRINTS:
 PR00775
PRODB:
 PRO_000022937
PROSITE:
 PS00298
REFSEQ:
 NP_415006
SMART:
 SM00387
SMR:
 P0A6Z3
UNIPROT:
 P0A6Z3


Operon      
Name: htpG         
Operon arrangement:
Transcription unit        Promoter
htpG
htpG
htpG


Transcriptional Regulation      
Display Regulation             
Repressed by: AscG


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_638 495076 forward nd [RS-EPT-CBR] [9]
  promoter TSS_639 495082 forward nd [RS-EPT-CBR] [9]
  promoter TSS_640 495090 forward nd [RS-EPT-CBR] [9]
  promoter TSS_641 497133 forward nd [RS-EPT-CBR] [9]


Evidence    

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


Reference(s)    

 [1] Bolon DN., 2012, Bound for observation., J Mol Biol 415(1):1-2

 [2] Buchner J., 2010, Bacterial Hsp90--desperately seeking clients., Mol Microbiol 76(3):540-4

 [3] Doyle SM., Hoskins JR., Kravats AN., Heffner AL., Garikapati S., Wickner S., 2019, Intermolecular Interactions between Hsp90 and Hsp70., J Mol Biol 431(15):2729-2746

 [4] Fauvet B., Finka A., Castanie-Cornet MP., Cirinesi AM., Genevaux P., Quadroni M., Goloubinoff P., 2021, Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates., Front Mol Biosci 8:653073

 [5] Pederson K., Chalmers GR., Gao Q., Elnatan D., Ramelot TA., Ma LC., Montelione GT., Kennedy MA., Agard DA., Prestegard JH., 2017, NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with 13 C-methyl alanine., J Biomol NMR 68(3):225-236

 [6] Shirai Y., Akiyama Y., Ito K., 1996, Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones., J Bacteriol 178(4):1141-5

 [7] Street TO., Lavery LA., Verba KA., Lee CT., Mayer MP., Agard DA., 2012, Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity., J Mol Biol 415(1):3-15

 [8] Ueguchi C., Ito K., 1992, Multicopy suppression: an approach to understanding intracellular functioning of the protein export system., J Bacteriol 174(5):1454-61

 [9] 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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