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Database: UniProt
Entry: A0A1L3MSF2_9BACI
LinkDB: A0A1L3MSF2_9BACI
Original site: A0A1L3MSF2_9BACI 
ID   A0A1L3MSF2_9BACI        Unreviewed;       466 AA.
AC   A0A1L3MSF2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=A9C19_11145 {ECO:0000313|EMBL:APH05266.1};
OS   Bacillus weihaiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH05266.1, ECO:0000313|Proteomes:UP000181936};
RN   [1] {ECO:0000313|EMBL:APH05266.1, ECO:0000313|Proteomes:UP000181936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alg07 {ECO:0000313|EMBL:APH05266.1,
RC   ECO:0000313|Proteomes:UP000181936};
RX   PubMed=27901120; DOI=10.1038/srep38248;
RA   Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT   "Complete genome sequence and transcriptomic analysis of a novel marine
RT   strain Bacillus weihaiensis reveals the mechanism of brown algae
RT   degradation.";
RL   Sci. Rep. 6:38248-38248(2016).
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}.
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DR   EMBL; CP016020; APH05266.1; -; Genomic_DNA.
DR   RefSeq; WP_072580058.1; NZ_CP016020.1.
DR   AlphaFoldDB; A0A1L3MSF2; -.
DR   STRING; 1547283.A9C19_11145; -.
DR   KEGG; bwh:A9C19_11145; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000181936; Chromosome.
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; 1.
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   Pfam; PF10431; ClpB_D2-small; 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:UP000181936}.
FT   DOMAIN          50..355
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          358..457
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          156..176
FT                   /note="Disordered"
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         279
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;  52338 MW;  D8D61C0C9B6E0E4A CRC64;
     MNKQLTPRQI VERLDQYIVG QKDAKKAVAV ALRNRYRRSL LNEKLREEVV PKNILMIGPT
     GVGKTEIARR IAKLSGAPFI KVEATKFTEV GYVGRDVESM VRDLVETSVR LVKEEKISEV
     KGTAEENANK RLVELLVPGK KKQAASKNPL EMFFGASSNQ NQEQDDSTVE ESSIQEKRRR
     IEHQLALGEL EDHYVTIEVE EQQASMFDML QGSGMEQMGM NMQDALGSFM PKKKKKRKLT
     VREARKVLTN EEASKLIDMD EVTSDAIIRA EQAGIIFIDE IDKIAGKSKG GSADVSREGV
     QRDILPIVEG STIVTKYGSV KTDHILFIAA GAFHIAKPSD LIPELQGRFP IRVELTKLSI
     DDFVKILVEP DNALLKQYSA LIETEGIQLE FSDDAIRKLA EVAYEVNQDT DNIGARRLHT
     IMERLLEDLS FEAPDITLEK IVITPQYVED KLGKISKNKD LSQFIL
//
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