ID   HSLU1_TRYB2             Reviewed;         475 AA.
AC   Q57VB1; D6XG90;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU1;
DE   AltName: Full=Mitochondrial proteasome-like protease HslVU ATPase subunit 1;
DE   Flags: Precursor;
GN   Name=HslU1; ORFNames=Tb927.5.1520;
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18421378; DOI=10.1371/journal.ppat.1000048;
RA   Li Z., Lindsay M.E., Motyka S.A., Englund P.T., Wang C.C.;
RT   "Identification of a bacterial-like HslVU protease in the mitochondria of
RT   Trypanosoma brucei and its role in mitochondrial DNA replication.";
RL   PLoS Pathog. 4:E1000048-E1000048(2008).
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC       subunit has chaperone activity. The binding of ATP and its subsequent
CC       hydrolysis by HslU are essential for unfolding of protein substrates
CC       subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC       its protein substrates and unfolds these before they are guided to HslV
CC       for hydrolysis (By similarity). The HslVU protease complex functions in
CC       mitochondrial DNA replication by regulating DNA helicase PIF2 protein
CC       levels. {ECO:0000250, ECO:0000269|PubMed:18421378}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC       side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC       complex (HslVU) is dependent on binding of ATP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast
CC       {ECO:0000269|PubMed:18421378}. Note=Associated with kinetoplast DNA
CC       (kDNA).
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC159443; AAX70437.1; -; Genomic_DNA.
DR   EMBL; CP000068; AAZ11267.1; -; Genomic_DNA.
DR   RefSeq; XP_844826.1; XM_839733.1.
DR   AlphaFoldDB; Q57VB1; -.
DR   SMR; Q57VB1; -.
DR   STRING; 5691.AAZ11267; -.
DR   PaxDb; Q57VB1; -.
DR   GeneID; 3657262; -.
DR   KEGG; tbr:Tb927.5.1520; -.
DR   VEuPathDB; TriTrypDB:Tb927.5.1520; -.
DR   eggNOG; KOG0745; Eukaryota.
DR   InParanoid; Q57VB1; -.
DR   OMA; KYGMIKT; -.
DR   BRENDA; 3.4.25.2; 6519.
DR   Proteomes; UP000008524; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0009376; C:HslUV protease complex; IDA:GeneDB.
DR   GO; GO:0020023; C:kinetoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:GeneDB.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IMP:GeneDB.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070581; P:rolling circle DNA replication; IDA:GeneDB.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48102:SF3; PTHR48102:SF3; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Kinetoplast; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..475
FT                   /note="ATP-dependent protease ATPase subunit HslU1"
FT                   /id="PRO_0000423755"
FT   BINDING         66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         108..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  52531 MW;  56A83B327B8C0DB1 CRC64;
     MMRRVTSSLP SALKLGRSLG PNVRFSGGAA AVEASPAIPP NSSSGKTLVR NMKPRELMQE
     LDNYIIGQTE AKKAVAVALR NRWRRHQVDA AIREEISPKN ILMIGPTGVG KTEIARRLAK
     LVDAPFIKVE ATKFTEVGFH GRDVESIIED LYKASLTQTK QNIMRRHEET ARQKAENRIL
     KALAGVSDGF REHLRSGALD DIEVIVELQE KKEKPKNSGT NEGVFISLEI PSSIGGQRPQ
     TVKKVMKIKD AIPAVLQEEL DKIVDTEDVS AEALRACEED GIVVIDEIDK IVTASGGYKG
     HQASAEGVQQ DLLPLVEGTT VSTKGNVQIK TDKILFICSG AFHSVKPSDM LAELQGRLPI
     RVELKPLTKE DFHRIITEPR YNLIKQHVMM MKTEGVDLVF TDDALWEIAS IAAHINSTVQ
     NIGARRLITI TEKVVEEVSF DGPDRKGETF VIDAAYVRNS VESMMKKVDI KKFIL