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Database: UniProt
Entry: A0A2S8SUR1_9BACT
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ID   A0A2S8SUR1_9BACT        Unreviewed;       466 AA.
AC   A0A2S8SUR1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=B1R32_10428 {ECO:0000313|EMBL:PQV64535.1};
OS   Abditibacterium utsteinense.
OC   Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC   Abditibacteriaceae; Abditibacterium.
OX   NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV64535.1, ECO:0000313|Proteomes:UP000237684};
RN   [1] {ECO:0000313|EMBL:PQV64535.1, ECO:0000313|Proteomes:UP000237684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV64535.1,
RC   ECO:0000313|Proteomes:UP000237684};
RX   PubMed=29475572;
RA   Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT   "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT   candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL   Syst. Appl. Microbiol. 0:0-0(2018).
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:PQV64535.1}.
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DR   EMBL; NIGF01000004; PQV64535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8SUR1; -.
DR   InParanoid; A0A2S8SUR1; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000237684; 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; 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:PQV64535.1};
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:PQV64535.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:PQV64535.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237684}.
FT   DOMAIN          51..355
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          358..447
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         62..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         279
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;  51456 MW;  E264EDB0638E9C90 CRC64;
     MSFHLLTPRQ IVAELDKYIV GQTAAKRAVA VALRNRFRRD QLSEDVRAGI IPRNILMIGP
     TGVGKTEIAR RLATLAGAPM LKIEATKFTE IGYVGREVDG IVRDLVEISI GMVEREKIAG
     VKDAARASAE ARLLDLLAPR PVRATNTAMP PNPFGAMWPQ AASAPTETER LQTEQNERLR
     SKLAEKLAAG EMEDAEVEFE IEEKRPSNIA FMAPGMEEGG DMSQMLSGLF PQNKKKRRLK
     VKDARPILEH QEAEMLLDRD AIISEAIARA QENGIVFLDE IDKIAGREGN GGPQVSREGV
     QRDLLPLVEG AVVNTKYGPV STEHMLFIAA GAFHVSKPSD LIPELQGRFP IRVELEPLTE
     EDLRRILTEP QGALINQYRA LLGADGVELE WTSDGISEIA RFAAQVNEST ENIGARRLHT
     LVEKVLEEVS FEAPEGEEKS VRINASFVRA RLAHLVSDDD LSRFIL
//
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