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Database: UniProt
Entry: K2GQY7_9BACI
LinkDB: K2GQY7_9BACI
Original site: K2GQY7_9BACI 
ID   K2GQY7_9BACI            Unreviewed;       464 AA.
AC   K2GQY7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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:EKE32799.1};
GN   ORFNames=MJ3_02537 {ECO:0000313|EMBL:EKE32799.1};
OS   Salimicrobium jeotgali.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX   NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32799.1, ECO:0000313|Proteomes:UP000011746};
RN   [1] {ECO:0000313|EMBL:EKE32799.1, ECO:0000313|Proteomes:UP000011746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ3 {ECO:0000313|EMBL:EKE32799.1,
RC   ECO:0000313|Proteomes:UP000011746};
RX   PubMed=23144427; DOI=10.1128/JB.01808-12;
RA   Lee S.H., Jung J.Y., Jeon C.O.;
RT   "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT   Myulchi-Jeot, Korean Fermented Seafood.";
RL   J. Bacteriol. 194:6695-6695(2012).
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:EKE32799.1}.
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DR   EMBL; AMPQ01000002; EKE32799.1; -; Genomic_DNA.
DR   RefSeq; WP_008587912.1; NZ_JAFBFF010000002.1.
DR   AlphaFoldDB; K2GQY7; -.
DR   STRING; 1230341.AAV35_007110; -.
DR   KEGG; sje:AAV35_007110; -.
DR   PATRIC; fig|1230341.3.peg.527; -.
DR   eggNOG; COG1220; Bacteria.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000011746; 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:EKE32799.1};
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:EKE32799.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:EKE32799.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011746}.
FT   DOMAIN          50..353
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          356..452
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          159..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         414
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   464 AA;  52438 MW;  2133CAFB77005B48 CRC64;
     MSVDLTPQKI VEKLDQYIIG QKEAKKSVAI ALRNRYRRMQ LDEDMRKEIV PKNILMIGPT
     GVGKTEVARR LAKLTNAPFI KVEATKFTEV GYVGRDVESM VRDLVEASIR VVKEEKTEGV
     QKKAEKQADK RLVKLLVPSS SEKQGPSMKN PFEMLFNQDS EEEEKEEDEA HDTKNKRQTV
     ERQLKNGELE DEMVTIEVEE SQAGAFDMFQ GSGMDQMGMN MQDAFSQFMP NKKKKRKLAV
     KDARKVLAQE EAQKMIDMDE VNQEAVNRVE QSGMIFIDEI DKVAAKGESQ GNVSREGVQR
     DILPIVEGST IMTKHGAVST DHILFIAAGA FHMSKPSDLI PELQGRFPIR VELHKLSVED
     FENILKEPQN ALLKQYKALL STEGIEINFT PEAITRLAEI AATVNRDTDN IGARRLHTIL
     EKLLEDLSFE APEVTMETIE ITPQYVDSKL SAIVDDKDLS RFIL
//
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