P11141

PR
Gene name
hsp-6
Protein name
Heat shock protein hsp-6
Names
Heat shock 70 kDa protein F, mitochondrial
Species
Caenorhabditis elegans
KEGG Pathway
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

603-657 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for P11141

Entry ID Method Resolution Chain Position Source
3DQG X-ray 172 A A/B/C/D 418-565 PDB
AF-P11141-F1 Predicted AlphaFoldDB

No variants for P11141

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P11141

No associated diseases with P11141

3 regional properties for P11141

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 36 - 43 IPR018181-1
conserved_site Heat shock protein 70, conserved site 221 - 234 IPR018181-2
conserved_site Heat shock protein 70, conserved site 362 - 376 IPR018181-3

Functions

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

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
heat shock protein binding Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
misfolded protein binding Binding to a misfolded protein.
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
unfolded protein binding Binding to an unfolded protein.

4 GO annotations of biological process

Name Definition
cellular response to unfolded protein Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
chaperone cofactor-dependent protein refolding The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
mitochondrial unfolded protein response The series of molecular signals generated as a consequence of the presence of unfolded proteins in the mitochondrial matrix; results in transcriptional upregulation of nuclear genes encoding mitochondrial stress proteins.
protein refolding The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P77319 hscC Chaperone protein HscC Escherichia coli (strain K12) PR
P0A6Y8 dnaK Chaperone protein DnaK Escherichia coli (strain K12) SS
P38646 HSPA9 Stress-70 protein, mitochondrial Homo sapiens (Human) SS
P09446 hsp-1 Heat shock protein hsp-1 Caenorhabditis elegans SS
10 20 30 40 50 60
MLSARSFLSS ARTIARSSLM SARSLSDKPK GHVIGIDLGT TNSCVSIMEG KTPKVIENAE
70 80 90 100 110 120
GVRTTPSTVA FTADGERLVG APAKRQAVTN SANTLFATKR LIGRRYEDPE VQKDLKVVPY
130 140 150 160 170 180
KIVKASNGDA WVEAQGKVYS PSQVGAFVLM KMKETAESYL GTTVNNAVVT VPAYFNDSQR
190 200 210 220 230 240
QATKDAGQIS GLNVLRVINE PTAAALAYGL DKDAGDKIIA VYDLGGGTFD VSILEIQKGV
250 260 270 280 290 300
FEVKSTNGDT FLGGEDFDHA LVHHLVGEFK KEQGVDLTKD PQAMQRLREA AEKAKCELSS
310 320 330 340 350 360
TTQTDINLPY ITMDQSGPKH LNLKLTRAKF EQIVGDLIKR TIEPCRKALH DAEVKSSQIA
370 380 390 400 410 420
DVLLVGGMSR MPKVQATVQE IFGKVPSKAV NPDEAVAMGA AIQGAVLAGD VTDVLLLDVT
430 440 450 460 470 480
PLSLGIETLG GIMTKLITRN TTIPTKKSQV FSTAADGQTQ VQIKVFQGER EMATSNKLLG
490 500 510 520 530 540
QFSLVGIPPA PRGVPQVEVT FDIDANGIVN VSARDRGTGK EQQIVIQSSG GLSKDQIENM
550 560 570 580 590 600
IKEAEKNAAE DAKRKELVEV INQAEGIIHD TEAKMTEFAD QLPKDECEAL RTKIADTKKI
610 620 630 640 650
LDNKDNETPE AIKEACNTLQ QQSLKLFEAA YKNMAAKNSG GDAQEAKTAE EPKKEQN