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Database: UniProt
Entry: A0A4Y7RN40_9FIRM
LinkDB: A0A4Y7RN40_9FIRM
Original site: A0A4Y7RN40_9FIRM 
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
//
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