HSP60_AJECA
ID HSP60_AJECA Reviewed; 590 AA.
AC P50142;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Heat shock protein 60, mitochondrial;
DE AltName: Full=Antigen HIS-62;
DE Flags: Precursor;
GN Name=HSP60;
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=1937804; DOI=10.1128/iai.59.12.4459-4464.1991;
RA Gomez F.J., Gomez A.M., Deepe G.S. Jr.;
RT "Protective efficacy of a 62-kilodalton antigen, HIS-62, from the cell wall
RT and cell membrane of Histoplasma capsulatum yeast cells.";
RL Infect. Immun. 59:4459-4464(1991).
RN [2]
RP SEQUENCE REVISION.
RA Gomez G.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May participate in assembly and/or disassembly of proteins
CC imported into the mitochondrion. HSP60 are ATPases and have affinity
CC for unfolded proteins.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; L11390; AAB46362.2; -; Genomic_DNA.
DR AlphaFoldDB; P50142; -.
DR SMR; P50142; -.
DR MoonProt; P50142; -.
DR PRIDE; P50142; -.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CAFA.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046812; F:host cell surface binding; IDA:CAFA.
DR GO; GO:0005178; F:integrin binding; IPI:CAFA.
DR GO; GO:0044650; P:adhesion of symbiont to host cell; IDA:CAFA.
DR GO; GO:1900036; P:positive regulation of cellular response to heat; IDA:CAFA.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding; Stress response;
KW Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..590
FT /note="Heat shock protein 60, mitochondrial"
FT /id="PRO_0000005040"
SQ SEQUENCE 590 AA; 61889 MW; ED1E2EDD55846E03 CRC64;
MQRALSSTSR ASVLSSAPTR APVSRFRSAG LSLQQQRFAH KELKFGVEGR AALLKGIDTL
AKAVCTTLGP KGRNVLIESS YGSPKITKDG VTVAKAVTLQ DKFENLGARL LQDVASKTNE
VAGDGTTTAT VLARAIFSET VKNVAAGCNP MDLRRGIQAA VEAVVEYLQA NKRDITTTEE
IAQVATISAN GDTHVGKLIS NAMEKVGKEG VITVKDGKTI EDELEVTEGM RFDRGYVSPY
FITDTKAQKV EFEKPLIVLS EKKISAVQDI IPALEASTTL RRPLVIIAED IEGEALAVCI
LNKLRGQLQV AAVKVPGFGD NRKSILGDIG ILTNATVFTD ELDMKLEKAT ADMLGSTGSI
TITKEDTIIL NGDGSKDSIA QRCEQIRGVI ADPTTSDYEK EKLQERLAKL SGGVAVIKVG
GASEVEVGEK KDRVVDALNA TRAAVEEGIL PGGGTALLKA AANGLASVKP TSSDQLRRIS
SLVSAITRPA RTIVENAGLE GSVIVGKLTD EHASDFNRGF DSAKGEYVDM IASGIVDPLK
VVRTALVDAS GVASLLGTTE VAIVEAPEEK GPAGPPGGMG GMGGMGGGMF
