ID A0A4Y7RN40_9FIRM Unreviewed; 464 AA.
AC A0A4Y7RN40;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=clpY {ECO:0000313|EMBL:TEB10159.1};
GN Synonyms=hslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN ORFNames=Pmgp_02564 {ECO:0000313|EMBL:TEB10159.1};
OS Pelotomaculum propionicicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=258475 {ECO:0000313|EMBL:TEB10159.1, ECO:0000313|Proteomes:UP000297597};
RN [1] {ECO:0000313|EMBL:TEB10159.1, ECO:0000313|Proteomes:UP000297597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGP {ECO:0000313|EMBL:TEB10159.1,
RC ECO:0000313|Proteomes:UP000297597};
RX PubMed=30126076; DOI=.1111/1462-2920.14388;
RA Hidalgo-Ahumada C.A.P., Nobu M.K., Narihiro T., Tamaki H., Liu W.T.,
RA Kamagata Y., Stams A.J.M., Imachi H., Sousa D.Z.;
RT "Novel energy conservation strategies and behaviour of Pelotomaculum
RT schinkii driving syntrophic propionate catabolism.";
RL Environ. Microbiol. 20:4503-4511(2018).
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:TEB10159.1}.
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DR EMBL; QFFZ01000031; TEB10159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y7RN40; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000297597; 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};
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:TEB10159.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:TEB10159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000297597}.
FT DOMAIN 49..353
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 356..455
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 60..65
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; 52720 MW; 3103AF080D1442CF CRC64;
MKDLTPRRIV EELDKYIVGQ NKAKKAVAVA LRNRYRRKLL SEDFRDEVIP KNILMIGPTG
VGKTEIARRL ARLVKAPFIK VEATKFTEVG YVGRDVESMV RDLVETAIRM VKQERLAIVQ
DRAERLANEK LVELLAPYPV QESPPRNPLE MLFGTSRQPE QIDMHQDQRV KRVQFEREIL
SEKLARGELE NEFIEIEVED NKPPMLEVFT GSGMEEMGVN LQDMLGGFLP KKKRKRKVTV
KEGRKILTQQ EAQKLIDMDE VTAAAVKRAE EDGIVFLDEI DKIAGREGYG PDVSRGGVQR
DILPIVEGST VMTKYGPVKT DHVLFVAAGA FHTSKPSDLI PELQGRFPIR VELESLTRED
FQQILTEPRN ALIKQYTELL AAEGVIVKFS QNSLVEIAEI AYTVNEQTEN IGARRLHTIL
EKLLEDISFE APELSGKEIE ISKEHVVEKL GELVKNEDLS RYIL
//