HS104_SCHPO
ID HS104_SCHPO Reviewed; 905 AA.
AC O94641;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Heat shock protein 104;
DE AltName: Full=Protein aggregation-remodeling factor hsp104;
GN Name=hsp104; ORFNames=SPBC16D10.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required, in concert with Hsp40 and Hsp70 and small Hsps, for
CC the dissociation, resolubilization and refolding of aggregates of
CC damaged proteins after heat or other environmental stresses. Extracts
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 components of the Hsp70/Hsp40
CC chaperone system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer, forming a ring with a central pore.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per
CC monomer. ATP binding to NBD1 triggers binding of polypeptides and
CC stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is
CC crucial for oligomerization (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C-terminal extension is involved in oligomerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB38512.1; -; Genomic_DNA.
DR PIR; T39572; T39572.
DR RefSeq; NP_596503.1; NM_001022424.2.
DR AlphaFoldDB; O94641; -.
DR SMR; O94641; -.
DR BioGRID; 276570; 35.
DR STRING; 4896.SPBC16D10.08c.1; -.
DR iPTMnet; O94641; -.
DR MaxQB; O94641; -.
DR PaxDb; O94641; -.
DR PRIDE; O94641; -.
DR EnsemblFungi; SPBC16D10.08c.1; SPBC16D10.08c.1:pep; SPBC16D10.08c.
DR GeneID; 2540026; -.
DR KEGG; spo:SPBC16D10.08c; -.
DR PomBase; SPBC16D10.08c; hsp104.
DR VEuPathDB; FungiDB:SPBC16D10.08c; -.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; O94641; -.
DR OMA; ERMKAVM; -.
DR PhylomeDB; O94641; -.
DR PRO; PR:O94641; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; EXP:PomBase.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IPI:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:PomBase.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:PomBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IMP:PomBase.
DR GO; GO:0043335; P:protein unfolding; IDA:PomBase.
DR Gene3D; 1.10.1780.10; -; 1.
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; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
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; PF02861; Clp_N; 2.
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 SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat; Stress response.
FT CHAIN 1..905
FT /note="Heat shock protein 104"
FT /id="PRO_0000372308"
FT DOMAIN 2..149
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..75
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 87..149
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 164..413
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 441..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..738
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 880..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 410..533
FT /evidence="ECO:0000255"
FT COMPBIAS 891..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 621..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 905 AA; 100507 MW; 564704277B6C5140 CRC64;
MADYPFTDKA AKTLSDAYSI AQSYGHSQLT PIHIAAALLS DSDSNGTTLL RTIVDKAGGD
GQKFERSVTS RLVRLPAQDP PPEQVTLSPE SAKLLRNAHE LQKTQKDSYI AQDHFIAVFT
KDDTLKSLLA EAGVTPKAFE FAVNNVRGNK RIDSKNAEEG FDALNKFTVD LTELARNGQL
DPVIGREDEI RRTIRVLSRR TKNNPVLIGE PGVGKTSIAE GLARRIIDDD VPANLSNCKL
LSLDVGSLVA GSKFRGEFEE RIKSVLKEVE ESETPIILFV DEMHLLMGAG SGGEGGMDAA
NLLKPMLARG KLHCIGATTL AEYKKYIEKD AAFERRFQII LVKEPSIEDT ISILRGLKEK
YEVHHGVTIS DRALVTAAHL ASRYLTSRRL PDSAIDLVDE AAAAVRVTRE SQPEVLDNLE
RKLRQLRVEI RALEREKDEA SKERLKAARK EAEQVEEETR PIREKYELEK SRGSELQDAK
RRLDELKAKA EDAERRNDFT LAADLKYYGI PDLQKRIEYL EQQKRKADAE AIANAQPGSE
PLLIDVVGPD QINEIVARWT GIPVTRLKTT EKERLLNMEK VLSKQVIGQN EAVTAVANAI
RLSRAGLSDP NQPIASFLFC GPSGTGKTLL TKALASFMFD DENAMIRIDM SEYMEKHSVS
RLIGAPPGYV GHEAGGQLTE QLRRRPYSVI LFDEIEKAAP EVLTVLLQVL DDGRITSGQG
QVVDAKNAVI IMTSNLGAEY LTTDNESDDG KIDSTTREMV MNSIRGFFRP EFLNRISSIV
IFNRLRRVDI RNIVENRILE VQKRLQSNHR SIKIEVSDEA KDLLGSAGYS PAYGARPLNR
VIQNQVLNPM AVLILNGQLR DKETAHVVVQ NGKIFVKPNH EANANGSADI DMDGIDDDVN
DEELE
