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Database: UniProt
Entry: N4WQ34_9BACI
LinkDB: N4WQ34_9BACI
Original site: N4WQ34_9BACI 
ID   N4WQ34_9BACI            Unreviewed;       466 AA.
AC   N4WQ34;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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:ENH98247.1};
GN   ORFNames=J416_00839 {ECO:0000313|EMBL:ENH98247.1};
OS   Gracilibacillus halophilus YIM-C55.5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH98247.1, ECO:0000313|Proteomes:UP000012283};
RN   [1] {ECO:0000313|EMBL:ENH98247.1, ECO:0000313|Proteomes:UP000012283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH98247.1,
RC   ECO:0000313|Proteomes:UP000012283};
RA   Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT   "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT   halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL   Submitted (MAR-2013) 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:ENH98247.1}.
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DR   EMBL; APML01000004; ENH98247.1; -; Genomic_DNA.
DR   RefSeq; WP_003462923.1; NZ_APML01000004.1.
DR   AlphaFoldDB; N4WQ34; -.
DR   STRING; 1308866.J416_00839; -.
DR   PATRIC; fig|1308866.3.peg.171; -.
DR   eggNOG; COG1220; Bacteria.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000012283; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
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:ENH98247.1};
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:ENH98247.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:ENH98247.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012283}.
FT   DOMAIN          50..359
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          358..454
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         280
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;  53409 MW;  2073E4EEED1280CD CRC64;
     MSMDFTPKQI VAKLDEYIIG QKEAKKSVAV ALRNRYRRMQ LPEEMRNEIV PKNILMIGPT
     GVGKTEVARR MANLVGAPFV KVEATKFTEV GYVGRDVESM VRDLVETSAR MVKEEEMEKV
     RDKAEEQANQ RMVKIMVPDK TKNKQSSMKN PFEMFMQNQT ADHDETETDE DQQNKKQRRE
     QTKRLLELGE LEDKVISIEV EEQSSSMSDM FQGSGMEQMG ANFQDMLSQF MPKKKKQRKL
     PVREARKILT QQEAQKLIDQ DEVNQKAIER VEQTGIIFID EMDKVAAKQE QSANVSREGV
     QRDILPIVEG STVMTKYGSV KTDHILFIAS GAFHMAKPSD LIPELQGRFP IRVEFDKLTV
     ADFERILREP SNALLRQYQA LLETEGITIS FTEEAVRRLA HIAHEVNQEM DNIGARRLHT
     ILEKLLEELS FEASDIGMGN IEITEAYVDE KLKEIATNQD LSQYIL
//
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