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Database: UniProt
Entry: W4PX27_9BACI
LinkDB: W4PX27_9BACI
Original site: W4PX27_9BACI 
ID   W4PX27_9BACI            Unreviewed;       463 AA.
AC   W4PX27;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=JCM9140_158 {ECO:0000313|EMBL:GAE24245.1};
OS   Halalkalibacter wakoensis JCM 9140.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE24245.1, ECO:0000313|Proteomes:UP000018890};
RN   [1] {ECO:0000313|EMBL:GAE24245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE24245.1};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT   wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(2014).
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:GAE24245.1}.
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DR   EMBL; BAUT01000001; GAE24245.1; -; Genomic_DNA.
DR   RefSeq; WP_034740931.1; NZ_BAZN01000001.1.
DR   AlphaFoldDB; W4PX27; -.
DR   STRING; 1236970.JCM9140_158; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000018890; 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   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:GAE24245.1};
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:GAE24245.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:GAE24245.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018890}.
FT   DOMAIN          50..352
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          355..451
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;  52193 MW;  3C2F34FF59B5C823 CRC64;
     MKTNLTPREI VSRLNQFIVG QEEAKKSVAI ALRNRYRRSL LEGKMKDEIT PKNILMIGPT
     GVGKTEIARR LAKLVGAPFV KVEATKFTEV GYVGRDVESM IRDLVETSVR IVKEEKAHKV
     RAQAETNANE RIVELLVPKV KKQSTYKNPL EMLFGQQGTE EVESDQTEDN NIEQRRRQMA
     HKLALGELED HMVTVEMDEQ SQGFMDMFQG QGMEQMGMNM QEMLGGMLPK KKKKKRLPVS
     DARKVLIDEE AQKLIDMDEV TQEAVTRAEQ LGIIFIDEID KVASKGQQSA DVSREGVQRD
     ILPIVEGSTV VTKHGSVKTD HILFIGAGAF HIAKPSDLIP ELQGRFPIRV ELSNLSIEDF
     KRILVEPNNA LIKQYVALLE TEGIKVTFSD EAVHKIATIA TEVNQETENI GARRLHTILE
     RLLEDLSFEA PDITLEEIVI TPEYVDEKLA SIAKNRDLSQ FIL
//
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