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Database: UniProt
Entry: A0A5C8P2T2_9BACI
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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
//
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