Q6MNF8

PR
Gene name
dnaK
Protein name
Chaperone protein DnaK
Names
HSP70, Heat shock 70 kDa protein, Heat shock protein 70
Species
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
KEGG Pathway
bba:Bd1298
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

564-637 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q6MNF8

Entry ID Method Resolution Chain Position Source
AF-Q6MNF8-F1 Predicted AlphaFoldDB

No variants for Q6MNF8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6MNF8

No associated diseases with Q6MNF8

3 regional properties for Q6MNF8

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 7 - 14 IPR018181-1
conserved_site Heat shock protein 70, conserved site 188 - 201 IPR018181-2
conserved_site Heat shock protein 70, conserved site 329 - 343 IPR018181-3

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
unfolded protein binding Binding to an unfolded protein.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGKIIGIDLG TTNSCVAIME GGEPKVLVNE EGARTTPSVV AYTKDGDRLV GQIAKRQAVT
70 80 90 100 110 120
NPENTIYSAK RFIGRRFEEI QEEIKLVPYT VVAKGNDCAF KVQGKTASPE EIGAAVLAKL
130 140 150 160 170 180
KKVAEDYLGE PVTEAVVTVP AYFNDAQRQA TKDAGRIAGL EVKRIINEPT AAALAYGMDK
190 200 210 220 230 240
KKDEKIVIYD FGGGTFDVSI LEVGDGVVEV RATNGDTHLG GDNFDTVILE WLITEFKKDQ
250 260 270 280 290 300
AIDLKNDKMA LQRLKEAAEK AKIELSSAQE TEINLPFITA DQSGPKHLQT RLSRAKFDQM
310 320 330 340 350 360
TEDLVKRSME PCRKALADSG LKASEIDEVV LVGGSTRIPA IQKAVKDFFG KEPNRSVNPD
370 380 390 400 410 420
EVVAIGAAVQ GGVLAGDVKD VLLLDVTPLS LGIETLGGVM TTLIERNTAI PSKKSQVFST
430 440 450 460 470 480
AADNQPAVDI HVLQGERKMA GDNKTLGRFE LVGIPPAPRG VPQVEVTFDI DANGILHVSA
490 500 510 520 530 540
KDMSSGKSQQ IKITAQSGMS EDEIKRAVAD AEGHAEEDKR KAEAATQRNN LDNLVYQTEK
550 560 570 580 590 600
LIKDSGAQLP ESEVKSANEA VAEAKKILEN KSASGDELKG AFERLQNLTH KLTSELYKKQ
610 620 630
GAQPGAEGQQ ADAAEGGEAS ANKGGDDVID ADYKDVN