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Database: UniProt
Entry: A0A5J5HXP4_9BACI
LinkDB: A0A5J5HXP4_9BACI
Original site: A0A5J5HXP4_9BACI 
ID   A0A5J5HXP4_9BACI        Unreviewed;       468 AA.
AC   A0A5J5HXP4;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-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:KAA9025884.1};
GN   ORFNames=F4V44_08340 {ECO:0000313|EMBL:KAA9025884.1};
OS   Niallia endozanthoxylica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=2036016 {ECO:0000313|EMBL:KAA9025884.1, ECO:0000313|Proteomes:UP000326671};
RN   [1] {ECO:0000313|EMBL:KAA9025884.1, ECO:0000313|Proteomes:UP000326671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MER_TA_151 {ECO:0000313|EMBL:KAA9025884.1,
RC   ECO:0000313|Proteomes:UP000326671};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Whole genome sequences of isolates from the Mars Exploration Rovers.";
RL   Submitted (SEP-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:KAA9025884.1}.
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DR   EMBL; VYKL01000015; KAA9025884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J5HXP4; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000326671; 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:InterPro.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000326671}.
FT   DOMAIN          52..357
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          360..454
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          155..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         63..68
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         346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         418
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   468 AA;  52154 MW;  8D86A8E0945873DC CRC64;
     MVKGINLTPR QIVERLNQYI IGQNDAKKAV AVALRNRYRR SLLDEKIRDE ISPKNILMIG
     PTGVGKTEIA RRIARLVQAP FVKVEATKFT EVGYVGRDVE SMVRDLIETS VRLVKEEKMQ
     SVKGKAEKNA NQRLVELLVP SNKKTASIKN PLEMLFGGGG NQDQQETSGS DEANLQEKRK
     SVLAKLAAGE LENEIVTVEV EENQPSMFDM LQGSGMEQMG LNMQDALGSL MPKRRKKRKL
     AVHEARKVLT QEEAAKLIDM DEVTQEAVYR AEQSGIIFID EIDKIASKNS GGSSADVSRE
     GVQRDILPIV EGSTVVTKYG SVKTDHILFI AAGAFHIAKP SDLIPELQGR FPIRVELTKL
     TIEDFVKILI EPDNALIKQY QALMATEGIQ IEFSDDAITK IAEVAFEVNQ NTDNIGARRL
     HTILEKLLED LSFEAAEITM EKIVITPQYV EEKLGAISRN KDLSRFIL
//
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