HSP78_CANAL
ID HSP78_CANAL Reviewed; 812 AA.
AC Q96UX5; A0A1D8PGX8; Q5AHB4;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heat shock protein 78, mitochondrial;
DE Flags: Precursor;
GN Name=HSP78; OrderedLocusNames=CAALFM_C203390CA;
GN ORFNames=CaO19.8501, CaO19.882;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RA Bhattacherjee V., Hostetter M.;
RT "The Candida albicans HSP78 gene encoding a member of the ClpB family of
RT stress proteins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Required, in concert with mitochondrial Hsp70, for the
CC dissociation, resolubilization and refolding of aggregates of damaged
CC proteins in the mitochondrial matrix after heat stress. May extract
CC proteins from aggregates by unfolding and threading them in an ATP-
CC dependent process through the axial channel of the protein hexamer,
CC after which they can be refolded by the Hsp70 chaperone system.
CC Required for resumption of mitochondrial respiratory function, DNA
CC synthesis and morphology after heat stress (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer, forming a ring with a central pore.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC monomer. NBD1 is primarily responsible for ATP hydrolysis. NBD2 is
CC crucial for oligomerization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AF399713; AAK97626.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27375.1; -; Genomic_DNA.
DR RefSeq; XP_721005.2; XM_715912.2.
DR AlphaFoldDB; Q96UX5; -.
DR SMR; Q96UX5; -.
DR BioGRID; 1220336; 1.
DR STRING; 237561.Q96UX5; -.
DR GeneID; 3637414; -.
DR KEGG; cal:CAALFM_C203390CA; -.
DR CGD; CAL0000189244; HSP78.
DR VEuPathDB; FungiDB:C2_03390C_A; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_5_0_1; -.
DR InParanoid; Q96UX5; -.
DR OrthoDB; 611758at2759; -.
DR PRO; PR:Q96UX5; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0070370; P:cellular heat acclimation; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response; Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..812
FT /note="Heat shock protein 78, mitochondrial"
FT /id="PRO_0000005499"
FT REGION 88..336
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 460..651
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT COILED 337..425
FT /evidence="ECO:0000255"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 534..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CONFLICT 27
FT /note="M -> I (in Ref. 1; AAK97626)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="L -> P (in Ref. 1; AAK97626)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="V -> G (in Ref. 1; AAK97626)"
FT /evidence="ECO:0000305"
FT CONFLICT 543..544
FT /note="GG -> LT (in Ref. 1; AAK97626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 91657 MW; A7C1CDB57C743267 CRC64;
MLSSRIPKGK LLKQTSATSY LNLAKSMPIT TARYRPNQYY ANELAKLNVF TIHNIPSPCF
SQVRNFHSSF PRKLQMQQTE QGDNRPALEK FGSDLTQLAK EGKLDPVIGR DHEIRRTIQI
LSRRTKNNPV LIGNAGTGKT AVMEGLAQRI IRGEVPDSMK DKQIITLDLA GIISGAKYRG
DFESKLKSIL KEVEEKNGKV ILFIDEFHLL MGLGKAEGSI DASNLLKPAL ARGKLSMCGA
TTIEEYRKYV EKDAALARRF SPVTVNEPTV EDTISILRGL KERYEVHHGV RIMDSALVTA
ALYSNRYITD RFLPDKAIDL VDEASSTLRL QHESRPDAIA TLDRQIMTIE IELESLRKEE
DQLSIDRKHK LEKELEVKKS ELKELTDQWE SEKRAIDAVK NAKSELEKAK YELEQATREG
DYARASRIQY ASIPELQDKI QELSKNELAA KSSNLLHDSV TSEDIAGVIS KMTGIPVNNL
LKGEKDKLLD MNILLRQSVV GQDEAIDAVS DAVRLQRAGL TSENRPIASF MFLGPTGTGK
TEGGKSLAQF LFNDKNAVVR FDMSEFQEKH TISRLIGSPP GYVGYEESGE LTEAVRRKPY
SVVLFDEFEK AHPDLSKLLL QVLDEGSLTD SHGKKIDFKN TIIVMTSNIG QEILLADKNT
YEDGHINSEV KSQVLENLRH HYAPEFLNRI DDIVVFNRLS KTALKEILDI RLREIGDRLV
DKRIILQLTD EAKTLLCDMG YDPTYGARPL NRVLRKKLLD PLAMRLIKGQ VQENETVKVE
VKDHKIYVVP NHSEGTVIEK EEDYFKEDKD DN
