HSLU_THEMA
ID HSLU_THEMA Reviewed; 463 AA.
AC Q9WYZ2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU;
DE AltName: Full=Unfoldase HslU;
GN Name=hslU; OrderedLocusNames=TM_0522;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12646382; DOI=10.1016/s0301-4622(02)00297-1;
RA Song H.K., Bochtler M., Azim M.K., Hartmann C., Huber R., Ramachandran R.;
RT "Isolation and characterization of the prokaryotic proteasome homolog HslVU
RT (ClpQY) from Thermotoga maritima and the crystal structure of HslV.";
RL Biophys. Chem. 100:437-452(2003).
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. {ECO:0000269|PubMed:12646382}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.
CC {ECO:0000269|PubMed:12646382};
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 is dependent on binding of ATP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35607.1; -; Genomic_DNA.
DR PIR; H72365; H72365.
DR RefSeq; NP_228332.1; NC_000853.1.
DR RefSeq; WP_004081401.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYZ2; -.
DR SMR; Q9WYZ2; -.
DR STRING; 243274.THEMA_02065; -.
DR EnsemblBacteria; AAD35607; AAD35607; TM_0522.
DR KEGG; tma:TM0522; -.
DR eggNOG; COG1220; Bacteria.
DR InParanoid; Q9WYZ2; -.
DR OMA; KYGMIKT; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
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:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00249; HslU; 1.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..463
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160555"
FT BINDING 21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 63..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 53052 MW; F871CD909FCBA5CA CRC64;
MKSFDEMTPK EIVQELDKYI VGQYEAKKAV AIAVRNRIRR QKLPEEWRKE VLPKNILMIG
PTGVGKTEIA RRLAQLSGSP FLKVEATRFT EVGYVGKNVD SMIRDLVEIS VNMVKQEKIK
EVERQAEELV EERILDALVP ESKAMPVVTN PFINLITGGQ QQQYTPEDRR RFRAKREEMR
EKLRKGELED EEIEIELEET VSPFMGIFGP GMEDLGIEIT NMFSGMLPKR KKKRKMKVSE
ARKVLLPLEA EKLIDMDKVV QEALDRAQNR GIIFIDEIDK IAGKESAVGP DVSRQGVQRD
LLPIVEGTTI MTKYGPVRTD FILFIAAGAF HVSRPSDLIP ELQGRFPIRV ELSPLTEEDF
VRILKEPENA IIKQYQALLS TEGVELVFTE DGIREMARIA YQLNQRLENI GARRLYTVAE
KVLEEISFEA PDIPEKRVVV DAEYVRRRLE KIVQDEDLSA YIL
