HSLV_TRYB2
ID HSLV_TRYB2 Reviewed; 209 AA.
AC Q383Q5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ATP-dependent protease subunit HslV;
DE EC=3.4.25.2;
DE AltName: Full=Mitochondrial proteasome-like protease HslVU protease subunit;
DE Flags: Precursor;
GN Name=HslV; ORFNames=Tb11.01.2000;
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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-20; THR-21 AND LYS-53.
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: Protease subunit of a proteasome-like degradation complex.
CC HslU recognizes protein substrates and unfolds these before guiding
CC them to HslV for hydrolysis. HslV is not believed to degrade folded
CC proteins (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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent cleavage of peptide bonds with broad
CC specificity.; EC=3.4.25.2; Evidence={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 peptidase T1B family. HslV subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00809}.
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DR EMBL; CH464491; EAN79976.1; -; Genomic_DNA.
DR RefSeq; XP_829088.1; XM_823995.1.
DR PDB; 4HNZ; X-ray; 2.39 A; A/B/C/D/E/F/G/H/I/J/K/L=20-191.
DR PDB; 4HO7; X-ray; 2.60 A; A/B/C=20-191.
DR PDBsum; 4HNZ; -.
DR PDBsum; 4HO7; -.
DR AlphaFoldDB; Q383Q5; -.
DR SMR; Q383Q5; -.
DR STRING; 5691.EAN79976; -.
DR MEROPS; T01.021; -.
DR PaxDb; Q383Q5; -.
DR GeneID; 3664228; -.
DR KEGG; tbr:Tb11.01.2000; -.
DR VEuPathDB; TriTrypDB:Tb927.11.10240; -.
DR eggNOG; ENOG502RS9W; Eukaryota.
DR InParanoid; Q383Q5; -.
DR BRENDA; 3.4.25.2; 6519.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0097014; C:ciliary plasm; IDA:GeneDB.
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:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:GeneDB.
DR GO; GO:0004175; F:endopeptidase activity; ISM:GeneDB.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:GeneDB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR GO; GO:0070581; P:rolling circle DNA replication; IDA:GeneDB.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; PTHR32194; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Kinetoplast; Mitochondrion; Protease;
KW Reference proteome; Threonine protease; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..209
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_0000423757"
FT ACT_SITE 20
FT /evidence="ECO:0000250"
FT MUTAGEN 20
FT /note="T->A: Strongly impairs peptidase activity."
FT /evidence="ECO:0000269|PubMed:18421378"
FT MUTAGEN 21
FT /note="T->A: Strongly impairs peptidase activity."
FT /evidence="ECO:0000269|PubMed:18421378"
FT MUTAGEN 53
FT /note="K->A: Strongly impairs peptidase activity."
FT /evidence="ECO:0000269|PubMed:18421378"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4HNZ"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4HNZ"
FT HELIX 69..85
FT /evidence="ECO:0007829|PDB:4HNZ"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:4HNZ"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4HNZ"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4HNZ"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:4HNZ"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:4HNZ"
SQ SEQUENCE 209 AA; 22684 MW; 32C071E15E358D81 CRC64;
MLRRVGRTTC SPAACQLRHT TILSVRKGDT VVLLGDRQVT LGERIVAKSS ACKLRRINDD
VVIGFAGSTA DAISLMEKLE NKIGEFPNQL TRAAVELAKE WRTDRALRRL EASLIVCSAE
ETLEIDGQGN VITPEADGIV AIGSGGTFAK AAARALIDVD GYDAEKIARK AMRIATDIDV
FSNEHWDVEV LKRKSEKQEG SEASAKTSE
