ID   HSLU2_TRYB2             Reviewed;         496 AA.
AC   Q382V8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU2;
DE   AltName: Full=Mitochondrial proteasome-like protease HslVU ATPase subunit 2;
DE   Flags: Precursor;
GN   Name=HslU2; ORFNames=Tb11.01.4050;
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; CH464491; EAN80173.1; -; Genomic_DNA.
DR   RefSeq; XP_829285.1; XM_824192.1.
DR   AlphaFoldDB; Q382V8; -.
DR   SMR; Q382V8; -.
DR   STRING; 5691.EAN80173; -.
DR   PaxDb; Q382V8; -.
DR   PRIDE; Q382V8; -.
DR   GeneID; 3665507; -.
DR   KEGG; tbr:Tb11.01.4050; -.
DR   VEuPathDB; TriTrypDB:Tb927.11.12230; -.
DR   eggNOG; KOG0745; Eukaryota.
DR   InParanoid; Q382V8; -.
DR   BRENDA; 3.4.25.2; 6519.
DR   Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR   GO; GO:0009376; C:HslUV protease complex; IDA:GeneDB.
DR   GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:GeneDB.
DR   GO; GO:0005739; C:mitochondrion; 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   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48102:SF2; PTHR48102:SF2; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF07728; AAA_5; 1.
DR   Pfam; PF10431; ClpB_D2-small; 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..10
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           11..496
FT                   /note="ATP-dependent protease ATPase subunit HslU2"
FT                   /id="PRO_0000423756"
FT   REGION          177..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  54897 MW;  FC19ABC5425B5032 CRC64;
     MIRFSWVRLC SSAMAAAAAS PDVQAITRAQ AMQLDDLSPR KIASILDSYI VGQAEGKRAV
     AISLRNRWRR RQIEDEGLRR DILPKNILLV GPTGVGKTEI SRRMAKLTEA PFVKVEATKY
     TEVGFKGKDV ESIIEDLYSN AKTKAKRRLE IEREKEAHEL ALEIVFNGWH SCRSASGSFG
     SSTRNSGSGD SSAEEDKNSS SRDNVTFEEF KEKYKTQFKD DMVVIDVTQQ PKGNTKPNAS
     INSVEMLSVG ILLGLGSESR GVKTRVTKRV EEALPLATQE ALSRLVDETQ ISALARTLAE
     QDGVVFIDEI DKVVTEPASA NADVSSTGVQ QDLLPLIEGS NVTLKDGSQI STDNILFICS
     GAFHTVKTSD MIAELQGRLP VRVEMHALKE EDIRRILCEP KFNLLLQQKA LMKTENIDLE
     FTPDAVDELA RVTTKVNANA QNIGARRLHT VVERVMDEYS FNCQDYEGKK VVIDAEVVRK
     ATGSLMNNID LAKYIL