ID HSLU_VIBCM Reviewed; 443 AA.
AC C3LSA3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249}; OrderedLocusNames=VCM66_2594;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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. {ECO:0000255|HAMAP-Rule:MF_00249}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00249}.
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DR EMBL; CP001233; ACP06890.1; -; Genomic_DNA.
DR RefSeq; WP_001293365.1; NC_012578.1.
DR AlphaFoldDB; C3LSA3; -.
DR SMR; C3LSA3; -.
DR KEGG; vcm:VCM66_2594; -.
DR HOGENOM; CLU_033123_0_0_6; -.
DR Proteomes; UP000001217; Chromosome I.
DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 CDD; cd19498; RecA-like_HslU; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00390; hslU; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT CHAIN 1..443
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_1000125455"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 60..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ SEQUENCE 443 AA; 49830 MW; 68D6377701045768 CRC64;
MSEMTPREIV SELNRHIIGQ DKAKRAVAIA LRNRWRRMQL EESLRVEVTP KNILMIGPTG
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVESII RDLTDVAVKL THQQAMEKVK
FRAEELAEER VLDALLPPPR DAWGQAEQKE ENSSTRQVFR KKLREGQLND KEIEINVAVP
QMGVEIMAPP GMEEMTNQLQ GLFQNLAGDT KKKRKMKIKD ALKALVEEEA AKLVNQEELK
EQAIYNVENN GIVFIDEIDK ICKRGEVSGP DVSREGGQRD LLPLIEGSTV STKHGMVRTD
HILFIASGAF QVAKPSDLIP ELQGRLPIRV ELEALSSNDF KRILTEPKAS LTEQYVALMK
TEQVDVQFTE DGIKQIADAA WQVNETTENI GARRLHTVLE RLMDEISFDA TEKAGQAFVI
DAAYVKARLG ELVEDEDLSR FIL
//
