ID A0A5C8P2T2_9BACI Unreviewed; 463 AA.
AC A0A5C8P2T2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
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:TXL67672.1};
GN ORFNames=FHP05_01260 {ECO:0000313|EMBL:TXL67672.1};
OS Cerasibacillus terrae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cerasibacillus.
OX NCBI_TaxID=2498845 {ECO:0000313|EMBL:TXL67672.1, ECO:0000313|Proteomes:UP000321574};
RN [1] {ECO:0000313|EMBL:TXL67672.1, ECO:0000313|Proteomes:UP000321574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-CFT480 {ECO:0000313|EMBL:TXL67672.1,
RC ECO:0000313|Proteomes:UP000321574};
RA Lin S.-Y., Tsai C.-F., Young C.-C.;
RT "Cerasibacillus sp. nov., isolated from maize field.";
RL Submitted (JUN-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:TXL67672.1}.
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DR EMBL; VDUW01000001; TXL67672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C8P2T2; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000321574; 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; 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:TXL67672.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:TXL67672.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000321574}.
FT DOMAIN 50..356
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 355..449
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 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 463 AA; 52898 MW; 6F77B76885A9A9FD CRC64;
MGMNYTPRQI VEQLDRYIIG QNNAKKSVAV ALRNRYRRTK LDDDMRDEII PKNILMIGPT
GVGKTEIARR LAKFISAPFI KVEATKFTEV GYVGRDVESM VRDLVEMSIR MVKEEKLSEV
NEKAEEKANK KLVTLLVPQV KKQTQMKNPF ELLFTGQQEN EEENEDVTDT QIKTKRKQIQ
QMLALGEMED HIVTIEIEET PPSLFDMLQG SGMEQMGMNM QDTFSKFMPK QKRKRKLPVS
EARKILTHQE AQRLIDMEEV SRDAIQRAEQ SGIIFVDEID KVAGKEDNSP NVSREGVQRD
ILPIVEGSTV ITKHGPVKTN HMLFIAAGAF HMAKPSDLIP ELQGRFPIRV ELEKLSVEDF
ERILREPSNA LLKQYEALLK TEGINIVFKD DAIESIAKIA YQVNQDTDNI GARRLHTILE
KLLEDLLFEA PDINLETVDV TSQYVNQKLS TIAKNKDLSQ YIL
//