hscA:Gene Product(s)
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Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
Standard name |
HscA |
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Synonyms |
DnaK-like molecular chaperone specific for IscU[1], B2526[2][1], Hsc[2][1], HscA[2][1], Hsc66[2][1] , ECK2523, hsc, JW2510, b2526 |
Product description |
chaperone, member of Hsp70 protein family[2][3] Hsc66, DnaK-like chaperone, specific for IscU; involved in FtsZ-ring formation; HscB is the J-like co-chaperone for HscA[4] |
EC number (for enzymes) |
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Notes
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
IDA: Inferred from Direct Assay |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0005524 |
ATP binding |
IDA: Inferred from Direct Assay |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0006457 |
protein folding |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006457 |
protein folding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016226 |
iron-sulfur cluster assembly |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016226 |
iron-sulfur cluster assembly |
IGI: Inferred from Genetic Interaction |
P |
Seeded from EcoCyc (v14.0) |
Missing: with/from | |||
GO:0016226 |
iron-sulfur cluster assembly |
IMP: Inferred from Mutant Phenotype |
P |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0016887 |
ATPase activity |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016887 |
ATPase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016887 |
ATPase activity |
IDA: Inferred from Direct Assay |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0043531 |
ADP binding |
IDA: Inferred from Direct Assay |
F |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0051082 |
unfolded protein binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0070417 |
cellular response to cold |
IEP: Inferred from Expression Pattern |
P |
Seeded from EcoCyc (v14.0) |
complete | |||
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
Protein |
rplJ |
Experiment(s):EBI-878924, EBI-882104 | ||
Protein |
secA |
Experiment(s):EBI-878924 | ||
Protein |
ygeQ |
Experiment(s):EBI-882104 | ||
Protein |
pepB |
Experiment(s):EBI-882104 | ||
Protein |
rplL |
Experiment(s):EBI-882104 | ||
Protein |
rplT |
Experiment(s):EBI-882104 | ||
Protein |
ugpB |
Experiment(s):EBI-882104 | ||
Protein |
rplQ |
Experiment(s):EBI-1143130 | ||
Protein |
rpsE |
Experiment(s):EBI-1143130 | ||
Protein |
ahpC |
Experiment(s):EBI-1143130 | ||
Protein |
rplE |
Experiment(s):EBI-1143130 | ||
Protein |
cheZ |
Experiment(s):EBI-1143130 | ||
Protein |
rpsC |
Experiment(s):EBI-1143130 | ||
Protein |
cedA |
Experiment(s):EBI-1143130 | ||
Protein |
chbA |
Experiment(s):EBI-1143130 | ||
Protein |
rpsI |
Experiment(s):EBI-1143130 | ||
Protein |
rpsD |
Experiment(s):EBI-1143130 | ||
Protein |
cybC |
Experiment(s):EBI-1143130 | ||
Protein |
ygjQ |
Experiment(s):EBI-1143130 | ||
Protein |
rplB |
Experiment(s):EBI-1143130 | ||
Protein |
rplF |
Experiment(s):EBI-1143130 | ||
Protein |
gnsA |
Experiment(s):EBI-1143130 | ||
Protein |
rplN |
Experiment(s):EBI-1143130 | ||
Protein |
fliT |
Experiment(s):EBI-1143130 | ||
Protein |
rplJ |
LCMS(ID Probability):99.0 MALDI(Z-score):17.053160 | ||
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Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
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Sequence |
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLADHEGR HLLPSVVHYQ QQGHSVGYDA RTNAALDTAN TISSVKRLMG RSLADIQQRY PHLPYQFQAS ENGLPMIETA AGLLNPVRVS ADILKALAAR ATEALAGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD FDHLLADYIR EQAGIPDRSD NRVQRELLDA AIAAKIALSD ADSVTVNVAG WQGEISREQF NELIAPLVKR TLLACRRALK DAGVEADEVL EVVMVGGSTR VPLVRERVGE FFGRPPLTSI DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSYA EQDVKARMLA EQKVEAARVL ESLHGALAAD AALLSAAERQ VIDDAAAHLS EVAQGDDVDA IEQAIKNVDK QTQDFAARRM DQSVRRALKG HSVDEV |
Length |
616 |
Mol. Wt |
65.652 kDa |
pI |
4.9 (calculated) |
Extinction coefficient |
20,400 - 20,650 (calc based on 10 Y, 1 W, and 2 C residues) |
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Domains/Motifs/Modification Sites
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
Resource type | Source | Notes/Reference |
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
Name | URL | Comments |
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Tokumoto, U et al. (2002) Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. J. Biochem. 131 713-9 PubMed
- ↑ Hoff, KG et al. (2003) Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. J. Biol. Chem. 278 37582-9 PubMed
- ↑ Silberg, JJ et al. (2004) Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. J. Biol. Chem. 279 53924-31 PubMed
- ↑ Reyda, MR et al. (2009) A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly. Biochemistry 48 10782-92 PubMed
- ↑ 9.0 9.1 Silberg, JJ & Vickery, LE (2000) Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 275 7779-86 PubMed
- ↑ 10.0 10.1 Brehmer, D et al. (2001) Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nat. Struct. Biol. 8 427-32 PubMed
- ↑ Nakamura, M et al. (1999) Hyperproduction of recombinant ferredoxins in escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster. J. Biochem. 126 10-8 PubMed
- ↑ 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. 126 917-26 PubMed
- ↑ Lelivelt, MJ & Kawula, TH (1995) Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock. J. Bacteriol. 177 4900-7 PubMed
- ↑ 14.0 14.1 14.2 14.3 14.4 14.5 14.6 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
- ↑ 15.00 15.01 15.02 15.03 15.04 15.05 15.06 15.07 15.08 15.09 15.10 15.11 15.12 15.13 15.14 15.15 15.16 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
- ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
- ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
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