ID G0ENN5_BRAIP Unreviewed; 453 AA.
AC G0ENN5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 ECO:0000313|EMBL:AEM23115.1};
GN OrderedLocusNames=Bint_2511 {ECO:0000313|EMBL:AEM23115.1};
OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM23115.1, ECO:0000313|Proteomes:UP000008522};
RN [1] {ECO:0000313|EMBL:AEM23115.1, ECO:0000313|Proteomes:UP000008522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA Hafstrom T., Jansson D.S., Segerman B.;
RT "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT features in Brachyspira species and phage-mediated horizontal gene
RT transfer.";
RL BMC Genomics 12:395-395(2011).
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; CP002874; AEM23115.1; -; Genomic_DNA.
DR RefSeq; WP_014488920.1; NC_017243.1.
DR AlphaFoldDB; G0ENN5; -.
DR KEGG; bip:Bint_2511; -.
DR PATRIC; fig|1045858.4.peg.2513; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_12; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000008522; 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:AEM23115.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:AEM23115.1}.
FT DOMAIN 56..342
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 345..439
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 67..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 453 AA; 51221 MW; 9CE8A29453C69DF9 CRC64;
MSFDAKLESE LTPRKIVEAL DQYIIGQTEA KRSVAIALRN RYRRRHLPDD LRDEVAPKNI
ILIGPTGVGK TEIARRLAKL VNAPFIKVEA TKYTEVGYVG RDVESMVRDL VNVAIFDLKT
AMMKEVEKEA TEIALDKLAK LLLPSVKKEN DENISEEEAE KKKNAKEQIK KRIQNGDFDE
SYVEIKISSG NNRMFGIIPG MGFEESDMIQ SMVGSIMPTN KKHKRLRVKE AKKYLINEAS
ESLIDMDKIT SDALSLTENM GIIFLDEIDK IASGNKTDSA DVARHGVQRD LLPIVEGTTV
NTRYGPIKTD HILFIAAGAF HINKPSDLIP ELQGRFPIRV ELKALSKEDF KDILVNPKNA
ITKQYQELLK TEGVTIEFEE EALSAIADIA YNINTNVENI GARRLYTIME KVFEEISFSA
DEHKGEFIKI NADNIKESMK DIEDNRDISR YIL
//
