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
//