htpG:Gene Product(s): Difference between revisions

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|-
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!align=left {{table heading style}} |Standard name
!align=left |Standard name
||
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HtpG  
HtpG  
|-
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!align=left {{table heading style}} |Synonyms
!align=left |Synonyms
||
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molecular chaperone HSP90 family<ref name='LIB:Riley_2006'/>, B0473<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, HtpG<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, C62.5<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Hsp90<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
molecular chaperone HSP90 family<ref name='LIB:Riley_2006'/>, B0473<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, HtpG<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, C62.5<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Hsp90<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
|-
|-
!align=left {{table heading style}} |Product description
!align=left |Product description
||
||
HtpG<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
HtpG<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
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Heat shock chaperone, HSP90 family; has ATPase activity; binds RpoH; rpoH regulon; dimeric<ref name='LIB:EcoGene'/>
Heat shock chaperone, HSP90 family; has ATPase activity; binds RpoH; rpoH regulon; dimeric<ref name='LIB:EcoGene'/>
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!align=left {{table heading style}} |EC number (for enzymes)
!align=left |EC number (for enzymes)
||
||




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!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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complete  
complete  


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!|Partner Type!!Partner!!Notes!!References!!Evidence
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Experiment(s):EBI-1136800<br />  
Experiment(s):EBI-1136800<br />  


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!|Compartment!!Description!!Evidence!!Source!!Notes
!|Compartment!!Description!!Evidence!!Source!!Notes


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|-
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!align=left {{table heading style}} |Sequence
!align=left |Sequence
||
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[http://biocyc.org/ECOLI/sequence-aa?object=EG10461-MONOMER at EcoCyc]  
[http://biocyc.org/ECOLI/sequence-aa?object=EG10461-MONOMER at EcoCyc]  
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LLAERGTLED PNLFIRRMNQ LLVS</pre>  
LLAERGTLED PNLFIRRMNQ LLVS</pre>  
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!align=left {{table heading style}} |Length
!align=left |Length
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624
624
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!align=left {{table heading style}} |Mol. Wt
!align=left |Mol. Wt
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71.424 kDa
71.424 kDa
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!align=left {{table heading style}} |pI
!align=left |pI
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5.0 (calculated)
5.0 (calculated)
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!align=left {{table heading style}} |Extinction coefficient
!align=left |Extinction coefficient
||
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81,820 (calc based on 18 Y, 10 W, and  C residues)
81,820 (calc based on 18 Y, 10 W, and  C residues)


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<beststructure>
<beststructure>
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</beststructure>
</beststructure>
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!align=left {{table heading style}} |Models
!align=left |Models
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View models at:
View models at:
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* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)


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Revision as of 01:39, 9 January 2010

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
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

HtpG

Synonyms

molecular chaperone HSP90 family[1], B0473[2][1], HtpG[2][1], C62.5[2][1], Hsp90[2][1]

Product description

HtpG[2][3];

Component of molecular chaperone, HSP90 family[3]

Heat shock chaperone, HSP90 family; has ATPase activity; binds RpoH; rpoH regulon; dimeric[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(s) Evidence Code with/from Aspect Notes Status
GO:0042623

ATPase activity, coupled

PMID:9707442[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc [6]

complete

GO:0006457

protein folding

PMID:10931286[7]

NR

P

Seeded from EcoCyc 12.5 [8]

complete

GO:0005515

protein binding

PMID:15690043[9]

IPI: Inferred from Physical Interaction

UniProtKB:P0A8T7

F

Seeded from EcoCyc 12.5 [8]

complete

GO:0005515

protein binding

PMID:16606699[10]

IPI: Inferred from Physical Interaction

UniProtKB:P0A6Y8

F

Seeded from EcoCyc 12.5 [8]

complete

GO:0005515

protein binding

PMID:16606699[10]

IPI: Inferred from Physical Interaction

UniProtKB:P36553

F

Seeded from EcoCyc 12.5 [8]

complete

GO:0005515

protein binding

PMID:16606699[10]

IPI: Inferred from Physical Interaction

UniProtKB:Q46808

F

Seeded from EcoCyc 12.5 [8]

complete

GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc [6]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR003594
SP_KW:KW-0067
HAMAP:MF_00505

F

Seeded from EcoCyc 12.5 [8]

complete

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [8]

complete

GO:0006457

protein folding

GO_REF:0000002
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001404
HAMAP:MF_00505

P

Seeded from EcoCyc 12.5 [8]

complete

GO:0006950

response to stress

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0346

P

Seeded from EcoCyc [6]

complete

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded from EcoCyc [6]

complete

GO:0051082

unfolded protein binding

GO_REF:0000002
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001404
HAMAP:MF_00505

F

Seeded from EcoCyc 12.5 [8]

complete

GO:0006457

protein folding

PMID:10931286[7]

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0005829

cytosol

PMID:16858726[11]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [6]

complete

GO:0005886

plasma membrane

GO_REF:0000004
GO_REF:0000004
GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_KW:KW-0997
SP_KW:KW-1003
SP_SL:SL-0037

C

Seeded from EcoCyc [6]

complete

GO:0042623

ATPase activity, coupled

PMID:9707442[5]

IDA

F

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0009408

response to heat

PMID:8349564[12]

IEP: Inferred from Expression Pattern

P

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

Subunits of molecular chaperone, HSP90 family

could be indirect

Protein

rpoC

PMID:15690043[9]

Experiment(s):EBI-889372

Protein

hyfG

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

mcrB

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

pepB

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

rplB

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

rpmC

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

rpmG

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

rpsF

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

rpsG

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

ugpB

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

ycbW

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

yeaI

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

yggR

PMID:15690043[9]

Experiment(s):EBI-894374

Protein

hemF

PMID:16606699[10]

Experiment(s):EBI-1136800
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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 Source Notes
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Notes

Structure and Physical Properties

[back to top]


Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc 

MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA LSNPDLYEGD
GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS GTKSFLESLG SDQAKDSQLI
GQFGVGFYSA FIVADKVTVR TRAAGEKPEN GVFWESAGEG EYTVADITKE DRGTEITLHL
REGEDEFLDD WRVRSIISKY SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE
ITDEEYKEFY KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY
VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN ALTKRVLQML
EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL RFASTHTDSS AQTVSLEDYV
SRMKEGQEKI YYITADSYAA AKSSPHLELL RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF
QSVSKVDESL EKLADEVDES AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS
TDADEMSTQM AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA
LLAERGTLED PNLFIRRMNQ LLVS
Length

624

Mol. Wt

71.424 kDa

pI

5.0 (calculated)

Extinction coefficient

81,820 (calc based on 18 Y, 10 W, and 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.

Type Residues Description Notes
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<motif_map/>

Structure
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Structures

<beststructure> gene=htpG taxon=562,83333 </beststructure>

Models

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Structure figures

Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:EG10461-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A6Z3

PFAM (EcoliWiki Page)

PFAM:PF02518

RefSeq (EcoliWiki Page)

RefSeq:NP_415006


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Notes

Links

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References

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  1. ↑ 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. ↑ 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
  3. ↑ 3.0 3.1 3.2 3.3 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 Panaretou, B et al. (1998) ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17 4829-36 PubMed
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  7. ↑ 7.0 7.1 Thomas, JG & Baneyx, F (2000) ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36 1360-70 PubMed
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 8.7 8.8 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  9. ↑ 9.00 9.01 9.02 9.03 9.04 9.05 9.06 9.07 9.08 9.09 9.10 9.11 9.12 9.13 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  10. ↑ 10.0 10.1 10.2 10.3 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  11. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  12. ↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed

Categories

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