ID A0A4V3GYD8_9FIRM Unreviewed; 461 AA.
AC A0A4V3GYD8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=C7959_10964 {ECO:0000313|EMBL:TDX51940.1};
OS Orenia marismortui.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Orenia.
OX NCBI_TaxID=46469 {ECO:0000313|EMBL:TDX51940.1, ECO:0000313|Proteomes:UP000295832};
RN [1] {ECO:0000313|EMBL:TDX51940.1, ECO:0000313|Proteomes:UP000295832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSL 6dP {ECO:0000313|EMBL:TDX51940.1,
RC ECO:0000313|Proteomes:UP000295832};
RA Wrighton K.;
RT "Subsurface microbial communities from deep shales in Ohio and West
RT Virginia, USA.";
RL Submitted (MAR-2019) 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:TDX51940.1}.
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DR EMBL; SOEG01000009; TDX51940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3GYD8; -.
DR STRING; 926561.GCA_000379025_02967; -.
DR Proteomes; UP000295832; 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 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 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, ECO:0000313|EMBL:TDX51940.1};
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:TDX51940.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:TDX51940.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295832}.
FT DOMAIN 49..350
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 353..447
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 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 461 AA; 52646 MW; B6F1B6E8325CF8E9 CRC64;
MEELTPKEIV KRLDKYIIGQ NEAKKSVAVA IRNRYRRKKL PLDLKDEVVP KNILMIGSTG
VGKTEIARRL AKLVKAPFIK IEVTKFTEVG YVGRDVESMV RDLLEISIRM IKNEKIEKVE
DKADSLAEER ILDLLLPRPK SKNKNPFGAL FADDDREDSI LDVEREERFE NQREKLRERL
RLGDLDDRMV EIEVEDNPSQ MVEIFSGTGV EEMGVNFQDI FGGMFPGKKK KRRVSIEEAK
SIIKEQEAQK LIDMDEVSRE AIQRVEEAGI IFLDEIDKIA AKNSSSAPDV SRGGVQRDIL
PIVEGSTIMT KYGPVKTDHI LFIAAGAFHV ASPTDLVPEL QGRFPIRVEL SSLSKEDFKE
ILIKPENALI KQYKALLETE GIKIDFTEES IDELADIAFR VNEQTENIGA RRLHTIIEKL
LEEISFIAPE IEEKEVIIDR EYVKDKLDNI VQNKDLSKYI L
//