HSP77_CANAL
ID HSP77_CANAL Reviewed; 648 AA.
AC P83784; A0A1D8PHW3; Q59U57;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Heat shock protein SSC1, mitochondrial;
DE AltName: Full=Cytoplasmic antigenic protein 6;
DE AltName: Full=mtHSP70;
DE Flags: Precursor;
GN Name=SSC1; OrderedLocusNames=CAALFM_C207380WA;
GN ORFNames=CaO19.1896, CaO19.9452;
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 [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 [2]
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 [3]
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).
RN [4]
RP PROTEIN SEQUENCE OF 591-597, AND ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(2004).
CC -!- FUNCTION: Required for the translocation of transit peptide-containing
CC proteins from the inner membrane into the mitochondrial matrix in an
CC ATP-dependent manner. Constitutes the ATP-driven core of the motor and
CC binds the precursor preprotein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- MISCELLANEOUS: Has antigenic properties. Elicits a specific immune
CC response in systemic candidiasis human patients undergoing malignant
CC hematological disorders.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27736.1; -; Genomic_DNA.
DR RefSeq; XP_713153.1; XM_708060.2.
DR AlphaFoldDB; P83784; -.
DR SMR; P83784; -.
DR BioGRID; 1228280; 1.
DR STRING; 237561.P83784; -.
DR COMPLUYEAST-2DPAGE; P83784; -.
DR PRIDE; P83784; -.
DR GeneID; 3645232; -.
DR KEGG; cal:CAALFM_C207380WA; -.
DR CGD; CAL0000178007; SSC1.
DR VEuPathDB; FungiDB:C2_07380W_A; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P83784; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR PRO; PR:P83784; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Coiled coil; Direct protein sequencing;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Stress response;
KW Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..648
FT /note="Heat shock protein SSC1, mitochondrial"
FT /id="PRO_0000089306"
FT COILED 560..633
FT /evidence="ECO:0000255"
SQ SEQUENCE 648 AA; 69748 MW; FDE4AAEBEF3D1DA3 CRC64;
MLSARNSLKN ISRQFPKALT RAQSTAAAPT GPVIGIDLGT TNSAVAVMEG KTPKILENSE
GGRTTPSIVA FTKDGERLVG IPAKRQAVVN PSDTLFATKR LIGRRYEDPE VQRDINQVPY
KIVKHGNGDA WLEARGEQYS PQQIGGFILN KMKETAEAAL SKKVNSAVVT CPAYFNDAQR
QATKDAGKIV GLNVLRVINE PTAAALAYGL EKKDGEVVAV FDLGGGTFDV SILDIGAGVF
EVKSTNGDTH LGGEDFDIAL VRYIVDAFKK ESGIDLEKDK MAIQRIREAA EKAKIELSST
VSTEINLPFI TADASGPKHI NQKISRAQFE QLVEPLIKKT IEPCKKALKD AGLSTSDVSE
VILVGGMSRM PKVVETVKSI FGKEPSKGIN PDEAVAMGAA IQGGILAGEV KDVVLLDVTP
LSLGIETMGG VFARLISRNT TIPAKKSQIF STAAAGQTSV EIRVFQGERE LTRDNKLIGN
FTLSGIPPAP KGVPQIEVTF DIDTDGIIKV SARDKATNKD ASITVAGSSG LSDAEIEKMV
NDAEKFAESD KARREAIEFA NRADQLCNDT ENSLNEHKEK LSSESVQKVQ DQIQQLREIV
LKAQAGEEVS PEELKQKTEE LQNEAINLFK DLYKDGGESS GSSEQPKN
