ID Q8I0E1_LEIIN Unreviewed; 503 AA.
AC Q8I0E1; A0A2K4YMJ0; A0A381MAV7; A0A6L0WR76;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE SubName: Full=Putative heat shock protein HslVU, ATPase subunit HslU {ECO:0000313|EMBL:CAM65876.1};
DE SubName: Full=Regulatory subunit of the HslVU complex {ECO:0000313|EMBL:CAD19161.1};
GN Name=HSLU {ECO:0000313|EMBL:CAM65876.1};
GN Synonyms=hslU {ECO:0000313|EMBL:CAD19161.1};
GN ORFNames=LINJ_09_0380 {ECO:0000313|EMBL:CAM65876.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM65876.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAD19161.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MHOM/67/MA {ECO:0000313|EMBL:CAD19161.1};
RX PubMed=12446803;
RA Couvreur B., Wattiez R., Bollen A., Falmagne P., Le Ray D., Dujardin J.C.;
RT "Eubacterial HslV and HslU subunits homologs in primordial eukaryotes.";
RL Mol. Biol. Evol. 19:2110-2117(2002).
RN [2] {ECO:0000313|EMBL:CAD21590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MHOM/67/MA {ECO:0000313|EMBL:CAD21590.1};
RA Couvreur B., Wattiez R., Jean-Claude D., Alex B., Falmagne P., Le Ray D.;
RT "Eubacterial HslV and HslU subunits homologues in primordial eukaryotes.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAM65876.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65876.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [4] {ECO:0000313|EMBL:CAM65876.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65876.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [5] {ECO:0000313|EMBL:CAM65876.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65876.1};
RA Aslett M.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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DR EMBL; AJ421946; CAD19161.1; -; Genomic_DNA.
DR EMBL; AJ428521; CAD21590.1; -; mRNA.
DR EMBL; AJ428522; CAD21591.1; -; mRNA.
DR EMBL; FR796441; CAM65876.1; -; Genomic_DNA.
DR RefSeq; XP_001463511.1; XM_001463474.1.
DR AlphaFoldDB; Q8I0E1; -.
DR SMR; Q8I0E1; -.
DR STRING; 5671.Q8I0E1; -.
DR MEROPS; X20.005; -.
DR GeneID; 5066885; -.
DR KEGG; lif:LINJ_09_0380; -.
DR VEuPathDB; TriTrypDB:LINF_090007900; -.
DR eggNOG; KOG0745; Eukaryota.
DR InParanoid; Q8I0E1; -.
DR OMA; WAYFRRR; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000008153; Chromosome 9.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00390; hslU; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF2; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU2; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000008153};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:CAM65876.1}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..503
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014312136"
FT DOMAIN 83..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 395..494
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 503 AA; 55674 MW; 9521C3F2A326C67C CRC64;
MLRFPTRLLF CVATAASTPS PDVLQVTKEK ASKLDDLSPR AITKILDAYI VGQDAGKRAV
AIALRNRWRR RQLSDADLRK EVVPKNMLLI GPTGVGKTEI SRRMARITDA PFIKVEATKY
TEVGFKGKDV ESIIEDLYTN AKLKARRALE AERHAEALNM ALDTVYSAWS VSQRMRAMDR
SLLSTGKAEE VTAAAADDSA AEAEESQPQQ QQHNFEYFRE HYLDEPITND MVTIDINAPQ
APTKPPKEGG IDLQSVGMLL GLGGEPKRLK VSVTKRVADA VPLATQEALD KLIDEASVNT
LARALAEEEG VVFVDEIDKV VAEPSSANAD VSSTGVQQDL LPLIEGSNVT MKDGSVIATD
NILFICSGAF HVVKTSDMIA ELQGRLPVRV ELQALTEEDF RRILTEPKFN LLRQQEEMLK
TEKIDVVFTE DGVNELAKVT CAVNSQGQNI GARRLNTILE RVMDPYSFNC EEYEGKRVEI
NAKMVREATE KLQKNVNLAK YLL
//