位置:首页 > 蛋白库 > HSLU_THEYD
HSLU_THEYD
ID   HSLU_THEYD              Reviewed;         445 AA.
AC   B5YG00;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249}; OrderedLocusNames=THEYE_A1397;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) 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:0000255|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:0000255|HAMAP-
CC       Rule:MF_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000255|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; CP001147; ACI21757.1; -; Genomic_DNA.
DR   RefSeq; WP_012546464.1; NC_011296.1.
DR   RefSeq; YP_002249198.1; NC_011296.1.
DR   AlphaFoldDB; B5YG00; -.
DR   SMR; B5YG00; -.
DR   STRING; 289376.THEYE_A1397; -.
DR   PRIDE; B5YG00; -.
DR   EnsemblBacteria; ACI21757; ACI21757; THEYE_A1397.
DR   KEGG; tye:THEYE_A1397; -.
DR   PATRIC; fig|289376.4.peg.1359; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_0; -.
DR   InParanoid; B5YG00; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 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   PANTHER; PTHR48102:SF3; PTHR48102:SF3; 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; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..445
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000125453"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         60..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   445 AA;  50991 MW;  D072A041D7AA3769 CRC64;
     MENLTPKKIV EELDKFIIGQ ESAKKAVAIA LRNRFRRQLL PKELRDEILP KNILMIGPTG
     VGKTEIARRL ARLVNAPFVK VEASKFTEVG YVGRDVESII RDLTEVAMNM VKQEHTERVQ
     EKARQLAEER VLDILLPQPR YTRDMNEAEE RTRYKETREK LRKQLREGIL DERYIEIDLK
     EKVVPFGIIS NVAMEEIEIN LKEMLGSFLP EKVKRKKVKI PEAIQLFTQE EANKLIDMEK
     VTKEAIERVE QTGIVFIDEI DKIASRGSSY GPDVSREGVQ RDLLPIVEGS TVTTKYGPVK
     TDHILFIAAG AFHVAKPSDL IPELQGRFPI RVELNSLGKE EFVRILTEPD NALIKQYIAL
     LATEDVYLEF TQDGIEEIAD ISQQVNEKTE NIGARRLHTV MEKLLEDISF NASELKGQKI
     TIDAKFVREK LSEIIKSEDL SRYIL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024