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Database: UniProt
Entry: U5L8X5_9BACI
LinkDB: U5L8X5_9BACI
Original site: U5L8X5_9BACI 
ID   U5L8X5_9BACI            Unreviewed;       468 AA.
AC   U5L8X5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000256|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN   ORFNames=N288_09670 {ECO:0000313|EMBL:AGX03855.1};
OS   Bacillus infantis NRRL B-14911.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX03855.1, ECO:0000313|Proteomes:UP000017805};
RN   [1] {ECO:0000313|EMBL:AGX03855.1, ECO:0000313|Proteomes:UP000017805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX03855.1,
RC   ECO:0000313|Proteomes:UP000017805};
RA   Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT   "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT   potential to induce cardiac disease by antigenic mimicry.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000256|ARBA:ARBA00009771, ECO:0000256|HAMAP-Rule:MF_00249}.
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DR   EMBL; CP006643; AGX03855.1; -; Genomic_DNA.
DR   RefSeq; WP_009795910.1; NC_022524.1.
DR   AlphaFoldDB; U5L8X5; -.
DR   STRING; 1367477.N288_09670; -.
DR   KEGG; bif:N288_09670; -.
DR   PATRIC; fig|1367477.3.peg.1874; -.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000017805; 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:UniProtKB-KW.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Pfam; PF10431; ClpB_D2-small; 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 {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Hydrolase {ECO:0000313|EMBL:AGX03855.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AGX03855.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017805}.
FT   DOMAIN          52..357
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          360..454
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         63..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         418
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   468 AA;  52427 MW;  E5A7E9EB3436F2C3 CRC64;
     MSLSTNLTPR QIVERLDQYI IGQKDAKKAV AVALRNRYRR GLLEEAIRDE ISPKNILMIG
     PTGVGKTEIA RRMAKLVGAP FVKVEATKFT EVGYVGRDVE SMVRDLVETS VRLVKEEKMQ
     SVKERAEENA NRRIVDMLVP SGKKAASYKN PLEMLFGGGG GQQDQENEPA EDYSLTEKRK
     IAREKLAMGE LENELITVEV EEQQPSMFDM LQGSGMEQMG MNMQDALSGL MPKKRKKRKL
     TVREARKVLS NEEAQKLIDM DEVTQEAVFR AEQSGIIFID EIDKIASKSS GGSNADVSRE
     GVQRDILPIV EGSTVVTKYG SVKTDHVLFM AAGAFHIAKP SDLIPELQGR FPIRVELTKL
     TVEDFYKILV EPDNALTKQY TALLETEGIQ IEFSDDAIRR IAEVAYEVNQ NTDNIGARRL
     HTILEKLLED LSFEAPEISM GKVTITPQYV EEKLGAISRN KDLSQFIL
//
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