ID   HSLU_HAMD5              Reviewed;         443 AA.
AC   C4K5T0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=HDEF_1270;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ67923.1; -; Genomic_DNA.
DR   RefSeq; WP_015873714.1; NC_012751.1.
DR   AlphaFoldDB; C4K5T0; -.
DR   SMR; C4K5T0; -.
DR   STRING; 572265.HDEF_1270; -.
DR   PRIDE; C4K5T0; -.
DR   EnsemblBacteria; ACQ67923; ACQ67923; HDEF_1270.
DR   GeneID; 66260970; -.
DR   KEGG; hde:HDEF_1270; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_6; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000002334; Chromosome.
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   Gene3D; 3.40.50.300; -; 1.
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   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; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..443
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000204524"
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;  49792 MW;  EB8632F2CD11517E CRC64;
     MSDMTPSEIV KKLDDYIIGQ DDAKRAVAIA LRNRWRRMQL DTELRQEITP KNILMIGPTG
     VGKTEIARRL AKLAEAPFIK VEATKFTEVG YVGKEVESII RDLTDTAVKM VRHQAIEKMR
     DKAKELAQER ILDILVSPAR NSSGQVEGSQ NTSTARQFFL EPLIKGELNE QEIEIDLAVT
     PVDIEIMSPP GMEEMTNQLQ SMFQHMSSQK HKIRKMKIGD ALKLLIDEEA SKLVNPEELK
     QVAIHSVEQN GIVFIDEVDK ICRHGSKSTS DVSREGVQRD LLPLVEGCTV STKHGMVKTD
     HILFIASGAF QVAKPSDLIP ELQGRFPIRV ELKSLTPKDF ERILTEPSAS LTYQYKSLMK
     TEGIKIEFTK DGITSIAGAA GQVNENTENI GARRLHTILE RVMEDISYNA DKIKKKSITI
     DSKYVDTHLS KLINNEDLSR FIL