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CLOBH:DNAK

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Species (Taxon ID) Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). (441771)
Gene Name(s) dnaK (ECO:0000255 with HAMAP-Rule:MF_00332)
Protein Name(s) Chaperone protein DnaK (ECO:0000255 with HAMAP-Rule:MF_00332)

HSP70 (ECO:0000255 with HAMAP-Rule:MF_00332) Heat shock 70 kDa protein (ECO:0000255 with HAMAP-Rule:MF_00332) Heat shock protein 70 (ECO:0000255 with HAMAP-Rule:MF_00332)

External Links
UniProt A5I640
EMBL CP000727
AM412317
RefSeq YP_001255452.1
YP_001388688.1
ProteinModelPortal A5I640
SMR A5I640
STRING 413999.CBO2959
EnsemblBacteria ABS38429
GeneID 5184256
5400902
KEGG cbh:CLC_2855
cbo:CBO2959
PATRIC 19367991
eggNOG COG0443
HOGENOM HOG000228136
KO K04043
OMA FFGKDPH
OrthoDB EOG6JMMSV
BioCyc CBOT413999:GJ72-3055-MONOMER
CBOT441771:GIWX-2819-MONOMER
Proteomes UP000001986
UP000002409
GO GO:0005524
GO:0071475
GO:0071468
GO:0034605
GO:0006457
Gene3D 1.20.1270.10
2.60.34.10
HAMAP MF_00332
InterPro IPR012725
IPR018181
IPR029048
IPR029047
IPR013126
Pfam PF00012
PRINTS PR00301
SUPFAM SSF100920
SSF100934
TIGRFAMs TIGR02350
PROSITE PS00297
PS00329
PS01036

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006950

response to stress

PMID:21378058[1]

ECO:0000315

P

Figure 6 and Table 3. Both show that the dnaK mutants had a maximum growth rate lower than the wild type strain at various stresses (temperature, pH, etc.)

complete
CACAO 3853

GO:0071475

cellular hyperosmotic salinity response

PMID:21378058[1]

ECO:0000315

P

As seen in figure 6 and table 3, there was a large reduction in growth in the DnaK mutant strain of Clostridium botulinum as compared to the wild type strain of Clostridium botulinum when grown in both 3% and 3.5% NaCl concentrations.

complete
CACAO 4147

GO:0071468

cellular response to acidity

PMID:21378058[1]

ECO:0000315

P

As seen in table 3 and in figure 6, there was a reduction in growth in the DnaK mutant strain of Clostridium botulinum as compared to the wild type strain of Clostridium botulinum when put under the stress of being grown at a pH of 5 or 6.

complete
CACAO 4148

GO:0034605

cellular response to heat

PMID:21378058[1]

ECO:0000315

P

As seen in figure 6 and table 3, there was a large reduction in growth in the DnaK mutant strain of Clostridium botulinum as compared to the wild type strain of Clostridium botulinum when put under the stress of being grown at high temperatures (temperatures greater than 37°C). Also, as seen in figure 7, the DnaK mutant strain of Clostridium botulinum showed much less growth when put under a temperature gradient of 42 to 48°C when grown on TPGY plates.

complete
CACAO 4149

involved_in

GO:0071475

cellular hyperosmotic salinity response

PMID:21378058[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071468

cellular response to acidic pH

PMID:21378058[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21378058[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051787

misfolded protein binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:95835
PANTHER:PTN002321897
RGD:2843
UniProtKB:P11021

F

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
MGI:MGI:105384
PANTHER:PTN002321897

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
MGI:MGI:105384
PANTHER:PTN002321897
RGD:2843
RGD:621725
SGD:S000000004
SGD:S000000171
SGD:S000000905
SGD:S000001106
SGD:S000001556
SGD:S000002388
SGD:S000003571
SGD:S000003947
SGD:S000005153
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:P54652

F

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
PANTHER:PTN002321897
UniProtKB:P0DMV8
UniProtKB:P0DMV9

F

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:105384
PANTHER:PTN002321897
RGD:621725
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066

F

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
SGD:S000000004
SGD:S000000756
SGD:S000003806
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:P54652

P

Seeded From UniProt

complete

involved_in

GO:0034620

cellular response to unfolded protein

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
PANTHER:PTN002321897
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000184706
PANTHER:PTN002321897
RGD:621725
SGD:S000000905
UniProtKB:A5I640
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066

P

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
RGD:1311806
UniProtKB:K7NTP5
UniProtKB:O73885
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:Q8IB24

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
EcoGene:EG13653
PANTHER:PTN002321897
PomBase:SPAC664.11
RGD:621725
SGD:S000000004
SGD:S000000171
SGD:S000002388
SGD:S000003571
SGD:S000003806
SGD:S000005153
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11021
UniProtKB:P11142
WB:WBGene00002005

F

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
RGD:1593284
RGD:2840
SGD:S000001556
SGD:S000003571
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
PANTHER:PTN000453405
UniProtKB:P9WMJ9

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
FB:FBgn0266599
MGI:MGI:105384
MGI:MGI:96244
PANTHER:PTN002321897
PomBase:SPCC1739.13
RGD:1311806
RGD:2843
RGD:621725
SGD:S000000004
SGD:S000000905
SGD:S000001106
SGD:S000002388
SGD:S000003947
UniProtKB:O73885
UniProtKB:P08106
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066
UniProtKB:P22953
UniProtKB:Q27975
UniProtKB:Q8IB24
WB:WBGene00002005

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
PANTHER:PTN002321897
RGD:621725
SGD:S000001556
SGD:S000003947
TAIR:locus:2101222
TAIR:locus:2121022
TAIR:locus:2135897
TAIR:locus:2144801
UniProtKB:P08106
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:Q7SX63

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012725

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:IPR012725

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:IPR012725

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000084064

F

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

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

edit table

Notes

References

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

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Selby, K et al. (2011) Important role of class I heat shock genes hrcA and dnaK in the heat shock response and the response to pH and NaCl stress of group I Clostridium botulinum strain ATCC 3502. Appl. Environ. Microbiol. 77 2823-30 PubMed GONUTS page
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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