ID N4WQ34_9BACI Unreviewed; 466 AA.
AC N4WQ34;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, 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 ECO:0000313|EMBL:ENH98247.1};
GN ORFNames=J416_00839 {ECO:0000313|EMBL:ENH98247.1};
OS Gracilibacillus halophilus YIM-C55.5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH98247.1, ECO:0000313|Proteomes:UP000012283};
RN [1] {ECO:0000313|EMBL:ENH98247.1, ECO:0000313|Proteomes:UP000012283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH98247.1,
RC ECO:0000313|Proteomes:UP000012283};
RA Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL Submitted (MAR-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}.
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:ENH98247.1}.
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DR EMBL; APML01000004; ENH98247.1; -; Genomic_DNA.
DR RefSeq; WP_003462923.1; NZ_APML01000004.1.
DR AlphaFoldDB; N4WQ34; -.
DR STRING; 1308866.J416_00839; -.
DR PATRIC; fig|1308866.3.peg.171; -.
DR eggNOG; COG1220; Bacteria.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000012283; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
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 {ECO:0000256|HAMAP-Rule:MF_00249, ECO:0000313|EMBL:ENH98247.1};
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:ENH98247.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:ENH98247.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012283}.
FT DOMAIN 50..359
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 358..454
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 61..66
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 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 466 AA; 53409 MW; 2073E4EEED1280CD CRC64;
MSMDFTPKQI VAKLDEYIIG QKEAKKSVAV ALRNRYRRMQ LPEEMRNEIV PKNILMIGPT
GVGKTEVARR MANLVGAPFV KVEATKFTEV GYVGRDVESM VRDLVETSAR MVKEEEMEKV
RDKAEEQANQ RMVKIMVPDK TKNKQSSMKN PFEMFMQNQT ADHDETETDE DQQNKKQRRE
QTKRLLELGE LEDKVISIEV EEQSSSMSDM FQGSGMEQMG ANFQDMLSQF MPKKKKQRKL
PVREARKILT QQEAQKLIDQ DEVNQKAIER VEQTGIIFID EMDKVAAKQE QSANVSREGV
QRDILPIVEG STVMTKYGSV KTDHILFIAS GAFHMAKPSD LIPELQGRFP IRVEFDKLTV
ADFERILREP SNALLRQYQA LLETEGITIS FTEEAVRRLA HIAHEVNQEM DNIGARRLHT
ILEKLLEELS FEASDIGMGN IEITEAYVDE KLKEIATNQD LSQYIL
//