ID   CLP_TRYBB               Reviewed;         868 AA.
AC   P31543; Q7KA51;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Heat shock protein 100;
DE   AltName: Full=Protein CLP;
GN   Name=HSP100;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2185473; DOI=10.1073/pnas.87.9.3513;
RA   Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
RA   Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.,
RA   Clark W.P., Ross B., Squires C.L., Maurizi M.R.;
RT   "Conservation of the regulatory subunit for the Clp ATP-dependent protease
RT   in prokaryotes and eukaryotes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=STIB 367H / ILTAR1;
RX   PubMed=9719514; DOI=10.1016/s0166-6851(98)00056-5;
RA   Redpath M.B., Carnall N., Webb H., Courel M., Amorim A., Guther M.L.S.,
RA   Cardoso de Almeida M.L., Carrington M.;
RT   "Conservation of genetic linkage between heat shock protein 100 and
RT   glycosylphosphatidylinositol-specific phospholipase C in Trypanosoma brucei
RT   and Trypanosoma cruzi.";
RL   Mol. Biochem. Parasitol. 94:113-121(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11377739; DOI=10.1016/s0166-6851(01)00268-7;
RA   Maier A.G., Webb H., Ding M., Bremser M., Carrington M., Clayton C.;
RT   "The coatomer of Trypanosoma brucei.";
RL   Mol. Biochem. Parasitol. 115:55-61(2001).
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; M92325; AAA30173.1; -; Genomic_DNA.
DR   EMBL; AJ000080; CAA03906.1; -; Genomic_DNA.
DR   EMBL; AJ250726; CAB60084.1; -; Genomic_DNA.
DR   AlphaFoldDB; P31543; -.
DR   SMR; P31543; -.
DR   MEROPS; X20.001; -.
DR   PRIDE; P31543; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; Nucleotide-binding; Repeat.
FT   CHAIN           1..868
FT                   /note="Heat shock protein 100"
FT                   /id="PRO_0000191222"
FT   DOMAIN          4..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          8..75
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          83..144
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          159..407
FT                   /note="I"
FT   REGION          529..720
FT                   /note="II"
FT   BINDING         204..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         603..610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   868 AA;  96905 MW;  7E06D4AFE46E1881 CRC64;
     MAHSDRQCTN AAQTALSDAV ESARKHNNGF VDPAHLALVL FKNEDGLASR VLRKLNAGTV
     LEPLAARVGA LPEQRPRPRS ITFSSDGGCA QHRRAEANRV GDSLIAVDHL LIGLFECKEV
     EAIMKAAHAS KKAVEGALLE LRKGKKVTSE FQEENYQALE KYATDLCKLA EEGKLDPVIG
     RTDEVLRTIR VLSRRTKNNP ILIGEPGVGK TAIAEGIAQR IVRGDVPDTL LNTRLFSLDL
     GALIAGSSLR GEFEERLKSV LNEVKESSNG VILFIDEIHL VLGAGKSGGS MDAANLLKPM
     LARGELRTIG ATTLEEYRTY VEKDAAFERR FMPVYVTEPS VEECISILRG LKDRYEAHHG
     VQITDNAVVV AAQLANRYIT NRFMPDKAID LIDEACANVR VQLSSRPEAI DILERKKRQL
     EIEAKALERD KEAASRERLK LVKADIQRVE EELQPLVSKY NDERQRIDEL QEMQSRLDEK
     KKLERAVRDG KMDLAADLQY NVIPLIQDRI RSLKEDIERQ KATLVQEKVT EGDVAAVVAR
     WTGIPVVKLS QTDRERLLNL SMHLHRRVKG QDEAVERVAD AIIRARAGLS RPNSPTASFL
     FLGPTGVGKT ELVKAVAAEL FDDEKHMVRI DMSEYMEQHS VSRLIGAPPG YIGHDEGGQL
     TEPVRRRPHA VVLFDEVEKA HPNVYNVLLQ VLDDGRLTDS RGRTVDFSNT IIVMTSNLGS
     EHLLNPEETN ESYEVLRENV LAAVRSYFRP ELINRLDDIV VFRRLRTEDL RGVVDNLIAG
     VNERLKSSGF SVLLDDGVKD FILEHGHDAN MGARPLRRWI EKNIVTEIGR MLIAKELPPN
     STLRVSLPEG GNKLTFGVKR GLTSDEWE