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ECOLI:HTPG

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) htpG
Protein Name(s) Chaperone protein HtpG

Heat shock protein C62.5 Heat shock protein HtpG High temperature protein G

External Links
UniProt P0A6Z3
EMBL M38777
U82664
U00096
AP009048
PIR A28324
RefSeq NP_415006.1
YP_488764.1
PDB 1SF8
1Y4S
1Y4U
2GQ0
2IOP
2IOQ
2IOR
PDBsum 1SF8
1Y4S
1Y4U
2GQ0
2IOP
2IOQ
2IOR
ProteinModelPortal P0A6Z3
SMR P0A6Z3
DIP DIP-29797N
IntAct P0A6Z3
MINT MINT-1227806
STRING 511145.b0473
PhosSite P0809402
SWISS-2DPAGE P0A6Z3
PaxDb P0A6Z3
PRIDE P0A6Z3
EnsemblBacteria AAC73575
BAE76252
GeneID 12932977
945099
KEGG ecj:Y75_p0460
eco:b0473
PATRIC 32116103
EchoBASE EB0456
EcoGene EG10461
eggNOG COG0326
HOGENOM HOG000031989
InParanoid P0A6Z3
KO K04079
OMA AIYYITA
OrthoDB EOG65TRNM
PhylomeDB P0A6Z3
BioCyc EcoCyc:EG10461-MONOMER
ECOL316407:JW0462-MONOMER
EvolutionaryTrace P0A6Z3
PRO PR:P0A6Z3
Proteomes UP000000318
UP000000625
Genevestigator P0A6Z3
GO GO:0005829
GO:0005886
GO:0005524
GO:0042623
GO:0042802
GO:0006200
GO:0006974
GO:0006457
GO:0009408
Gene3D 3.30.565.10
HAMAP MF_00505
InterPro IPR003594
IPR019805
IPR001404
IPR020575
IPR020568
PANTHER PTHR11528
Pfam PF02518
PF00183
PIRSF PIRSF002583
PRINTS PR00775
SMART SM00387
SUPFAM SSF54211
SSF55874
PROSITE PS00298

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016887

ATPase activity

PMID:20727857[1]

ECO:0000314

F

Fig 2 shows ATPase activity in the presence of various proteins.

complete
CACAO 9616

enables

GO:0016887

ATPase activity

PMID:20727857[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001233
PANTHER:PTN000163527
PomBase:SPAC926.04c
SGD:S000004798
SGD:S000006161

F

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10461
PANTHER:PTN000163828

F

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10461
PANTHER:PTN000163828

P

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10461
PANTHER:PTN000163828

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
EcoGene:EG10461
PANTHER:PTN000163527
PomBase:SPAC926.04c
SGD:S000004798
SGD:S000006161
WB:WBGene00000915

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6Z3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18462680[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6Z3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6Z3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15837196[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6Z3

F

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:8349564[7]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:11967071[8]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:9707442[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:10931286[10]

ECO:0000269

experimental evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103197

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103197

C

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103197

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103197

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 Motojima-Miyazaki, Y et al. (2010) Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity. Biochem. Biophys. Res. Commun. 400 241-5 PubMed GONUTS page
  2. ↑ 2.0 2.1 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 GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  5. ↑ Krukenberg, KA et al. (2008) Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure 16 755-65 PubMed GONUTS page
  6. ↑ Huai, Q et al. (2005) Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13 579-90 PubMed GONUTS page
  7. ↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
  8. ↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
  9. ↑ 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 GONUTS page
  10. ↑ Thomas, JG & Baneyx, F (2000) ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36 1360-70 PubMed GONUTS page
  11. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  12. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
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