GenomeNet

Database: UniProt
Entry: B8KUS6_9GAMM
LinkDB: B8KUS6_9GAMM
Original site: B8KUS6_9GAMM 
ID   B8KUS6_9GAMM            Unreviewed;       433 AA.
AC   B8KUS6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
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:EED34343.1};
GN   ORFNames=NOR51B_280 {ECO:0000313|EMBL:EED34343.1};
OS   Luminiphilus syltensis NOR5-1B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Luminiphilus.
OX   NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34343.1, ECO:0000313|Proteomes:UP000004699};
RN   [1] {ECO:0000313|Proteomes:UP000004699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX   PubMed=23705883;
RA   Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT   "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT   OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT   syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT   Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT   halotolerans.";
RL   BMC Microbiol. 13:118-118(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS999411; EED34343.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8KUS6; -.
DR   STRING; 565045.NOR51B_280; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_6; -.
DR   Proteomes; UP000004699; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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};
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:UP000004699};
KW   Stress response {ECO:0000313|EMBL:EED34343.1}.
FT   DOMAIN          46..320
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          323..421
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         57..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         309
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         381
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   433 AA;  48486 MW;  BE56846343B2628F CRC64;
     MTPREIVHEL DKHIVGQSDA KRAVAIALRN RWRRQQLDDE LRAEITPKNI LMIGPTGVGK
     TEIARRLARL AAAPFVKVEA TKFTEVGYVG RDVESMVRDL AETAIKMHRE QAMEKVQYRA
     EEAAEERLLD LLLPPDRDDS NTSTRQILRK KLREGDLDDR EVEIEITHQG ASVDIMAPPG
     MEEMTEQLQG LFSNLRPSGK SRRLPVKEAL KALVEEEAAK LINHDDLKAE ALEAAEQNGI
     IFIDELDKVA KRGEVGGADV SREGVQRDLL PLIEGCSVST KHGTIKTDHI LFIASGAFHL
     SKPSDLIPEL QGRLPIRVEL EALGSAEFQR ILTEPRSSLT EQNRALMATE GVELEFTEDG
     IRRLAEIAWQ VNEQAENIGA RRLHTVMERL LEEVSFTAAD AGLEQRQVVI DADFVDERLA
     SLAQNEDLSR FIL
//
DBGET integrated database retrieval system