RegulonDB RegulonDB 10.8: Gene Form
   

hscA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

hscA hscB fdx TSS_2826 TSS_2826 TSS_2825 TSS_2825 iscXp3 iscXp3

Gene      
Name: hscA    Texpresso search in the literature
Synonym(s): ECK2523, EG12130, b2526, hsc
Genome position(nucleotides): 2657085 <-- 2658935 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 57.7
External database links:  
ASAP:
 ABE-0008315
CGSC:
 32977
ECHOBASE:
 EB2051
OU-MICROARRAY:
 b2526
PortEco:
 hscA
STRING:
 511145.b2526
COLOMBOS: hscA


Shine dalgarno      
Sequence: ttttaatttcTGGAAGctaaaCAT


Product      
Name: iron-sulfur cluster biosynthesis chaperone HscA
Synonym(s): Hsc, Hsc66, HscA, chaperone for [Fe-S] cluster biosynthesis, chaperone, member of Hsp70 protein family
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 65.652
Isoelectric point: 4.762
Motif(s):
 
Type Positions Sequence
22 -> 600 AGIDLGTTNSLVATVRSGQAETLADHEGRHLLPSVVHYQQQGHSVGYDARTNAALDTANTISSVKRLMGRSLADIQQRYPHLPYQFQASENGLPMIETAAGLLNPVRVSADILKALAARATEALAGELDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLLADYIREQAGIPDRSDNRVQRELLDAAIAAKIALSDADSVTVNVAGWQGEISREQFNELIAPLVKRTLLACRRALKDAGVEADEVLEVVMVGGSTRVPLVRERVGEFFGRPPLTSIDPDKVVAIGAAIQADILVGNKPDSEMLLLDVIPLSLGLETMGGLVEKVIPRNTTIPVARAQDFTTFKDGQTAMSIHVMQGERELVQDCRSLARFALRGIPALPAGGAHIRVTFQVDADGLLSVTAMEKSTGVEASIQVKPSYGLTDSEIASMIKDSMSYAEQDVKARMLAEQKVEAARVLESLHGALAADAALLSAAERQVIDDAAAHLSEVAQGDDVDAIEQAIKNVDKQTQDFAARRM
456 -> 465 LRGIPALPAG
557 -> 557 A
516 -> 516 S
212 -> 212 T

 
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:1990230 - iron-sulfur cluster transfer complex
molecular_function GO:0051787 - misfolded protein binding
GO:0005515 - protein binding
GO:0016887 - ATPase activity
GO:0051082 - unfolded protein binding
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0031072 - heat shock protein binding
GO:0043531 - ADP binding
GO:0044183 - protein folding chaperone
biological_process GO:0006457 - protein folding
GO:0016226 - iron-sulfur cluster assembly
GO:0042026 - protein refolding
GO:0051085 - chaperone cofactor-dependent protein refolding
GO:0070417 - cellular response to cold
GO:0006986 - response to unfolded protein
GO:0034620 - cellular response to unfolded protein
GO:0097428 - protein maturation by iron-sulfur cluster transfer
Note(s): Note(s): ...[more].
Evidence: [IMP] Inferred from mutant phenotype
Reference(s): [1] Aoto PC., et al., 2005
[2] Iametti S., et al., 2015
[3] Okutani S., et al., 2015
[4] Takahashi Y., et al., 1999
[5] Tanaka N., et al., 2016
External database links:  
DIP:
 DIP-47348N
ECOCYC:
 EG12130-MONOMER
ECOLIWIKI:
 b2526
INTERPRO:
 IPR013126
INTERPRO:
 IPR042039
INTERPRO:
 IPR029048
INTERPRO:
 IPR029047
INTERPRO:
 IPR018181
INTERPRO:
 IPR010236
MODBASE:
 P0A6Z1
PANTHER:
 PTHR19375
PDB:
 1U00
PFAM:
 PF00012
PRIDE:
 P0A6Z1
PRINTS:
 PR00301
PRODB:
 PRO_000022925
PROSITE:
 PS00297
PROSITE:
 PS01036
PROSITE:
 PS00329
REFSEQ:
 NP_417021
SMR:
 P0A6Z1
SWISSMODEL:
 P0A6Z1
UNIPROT:
 P0A6Z1


Operon      
Name: hscBA-fdx-iscX         
Operon arrangement:
Transcription unit        Promoter
hscBA-fdx-iscX


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 iscXp3 2656917 reverse Similarity to the consensus
Read more > 		[ICWHO] [6]
  promoter TSS_2825 2658287 reverse nd [RS-EPT-CBR] [7]
  promoter TSS_2826 2658293 reverse nd [RS-EPT-CBR] [7]


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] Aoto PC., Ta DT., Cupp-Vickery JR., Vickery LE., 2005, X-ray diffraction analysis of a crystal of HscA from Escherichia coli., Acta Crystallogr Sect F Struct Biol Cryst Commun 61(Pt 7):715-7

 [2] Iametti S., Barbiroli A., Bonomi F., 2015, Functional implications of the interaction between HscB and IscU in the biosynthesis of FeS clusters., J Biol Inorg Chem 20(6):1039-48

 [3] Okutani S., Iwai T., Iwatani S., Matsuno K., Takahashi Y., Hase T., 2015, Response of Fe-S cluster assembly machinery of Escherichia coli to mechanical stress in a model of amino-acid crystal fermentation., J Biosci Bioeng 120(3):287-93

 [4] Takahashi Y., Nakamura M., 1999, Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli., J Biochem 126(5):917-26

 [5] Tanaka N., Kanazawa M., Tonosaki K., Yokoyama N., Kuzuyama T., Takahashi Y., 2016, Novel features of the ISC machinery revealed by characterization of Escherichia coli mutants that survive without iron-sulfur clusters., Mol Microbiol 99(5):835-48

 [6] 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

 [7] 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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