ID A0A140LAM7_9FIRM Unreviewed; 467 AA.
AC A0A140LAM7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=clpY {ECO:0000313|EMBL:KXG77602.1};
GN Synonyms=hslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN ORFNames=AN618_09720 {ECO:0000313|EMBL:KXG77602.1};
OS Fervidicola ferrireducens.
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Fervidicola.
OX NCBI_TaxID=520764 {ECO:0000313|EMBL:KXG77602.1, ECO:0000313|Proteomes:UP000070427};
RN [1] {ECO:0000313|EMBL:KXG77602.1, ECO:0000313|Proteomes:UP000070427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y170 {ECO:0000313|EMBL:KXG77602.1,
RC ECO:0000313|Proteomes:UP000070427};
RA Patel B.K.;
RT "Draft genome sequnece of Fervidicola ferrireducens strain Y170.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXG77602.1}.
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DR EMBL; LOED01000009; KXG77602.1; -; Genomic_DNA.
DR RefSeq; WP_066352739.1; NZ_LOED01000009.1.
DR AlphaFoldDB; A0A140LAM7; -.
DR STRING; 520764.AN618_09720; -.
DR PATRIC; fig|520764.3.peg.1009; -.
DR InParanoid; A0A140LAM7; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000070427; Unassembled WGS sequence.
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; IPR001270; ClpA/B.
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 PRINTS; PR00300; CLPPROTEASEA.
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:KXG77602.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:KXG77602.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070427}.
FT DOMAIN 49..354
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 357..455
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 60..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 467 AA; 53178 MW; 06A8CF4D7FBC2C8C CRC64;
MEDLTPRKIV EELDKYIVGQ QEAKRCVAIA LRNRYRRQKL PKELQDEIMP KNILMIGPTG
VGKTEIARRL AKLVNAPFVK VEATKFTEVG YVGRDVDSMV RDLVETSIRM VKAEKMEQVK
DRAKELAELR IAEILQPDPA KSSGFKNPFE VLFGNISRID ESDEEYESKL KMAKEKRKAL
LEDIKSGKLD NEMIEIEVED NSVPVLEVFS NYGIEEMGIN FQDLFGGLIP RRKKKKRVTI
ETARKILTQE EAQKLIDMDE VISEAIKRAE ETGIIFIDEI DKIAGREHGT GPDVSREGVQ
RDILPIVEGC TVVTKYGPVK TDHILFIAAG AFHISKPSDL IPELQGRFPI RVELKSLSKE
DLKRILVEPK NSLIKQYKAL LETEGIKIHF TEDAIDEIVS IAAHVNQHTE NIGARRLHTI
MEKLLEDISF NASEIKENSP EFVIDKNYVD EKLKDIVKDK DLSMYIL
//