C5CU12

PR
Gene name
dnaK
Protein name
Chaperone protein DnaK
Names
HSP70, Heat shock 70 kDa protein, Heat shock protein 70
Species
Variovorax paradoxus (strain S110)
KEGG Pathway
vap:Vapar_1712
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

572-645 (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 C5CU12

Entry ID Method Resolution Chain Position Source
AF-C5CU12-F1 Predicted AlphaFoldDB

No variants for C5CU12

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5CU12

No associated diseases with C5CU12

3 regional properties for C5CU12

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 193 - 206 IPR018181-2
conserved_site Heat shock protein 70, conserved site 338 - 352 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
MAKIIGIDLG TTNSCVSIME GNTTRVIENS EGARTTPSIV AYQEDGEVLV GASAKRQAVT
70 80 90 100 110 120
NPKNTLYAIK RLIGRKFEEK EVQKDIDLMP YTIAKADNGD AWVEVRGKKI APQQVSADIL
130 140 150 160 170 180
RKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
190 200 210 220 230 240
LDKQDKADRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
250 260 270 280 290 300
IIAEFKKEQG VDLGKDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
310 320 330 340 350 360
LTRAKLESLV DELVERTIAP CRLAIKDAGI SVSDINDVIL VGGMTRMPKV QEKVKAFFGK
370 380 390 400 410 420
EPRKDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETMGGVMT KMITKNTTIP
430 440 450 460 470 480
TKFAQTFSTA EDNQPAVTIK VFQGEREIAS GNKLLGEFNL EGIPPAARGT PQIEVSFDID
490 500 510 520 530 540
ANGILHVGAK DKGTGKENKI TIKANSGLSE DEIQKMVKDA ELNAAEDKKK VELAQARNQG
550 560 570 580 590 600
EAMVHSVKKS LGEHGASLDA GEKEKIEAAI KDLEEALKGE DKASIEEKTN TLMTASQKLG
610 620 630 640
EKMYADAQAA AGAAGGPGAA AGPEAASAPA DDNVVDAEVK EVKKG