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Database: UniProt
Entry: A0A154BTP4_ANASB
LinkDB: A0A154BTP4_ANASB
Original site: A0A154BTP4_ANASB 
ID   A0A154BTP4_ANASB        Unreviewed;       461 AA.
AC   A0A154BTP4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AXX12_04005 {ECO:0000313|EMBL:KYZ77302.1};
OS   Anaerosporomusa subterranea.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Anaerosporomusa.
OX   NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ77302.1, ECO:0000313|Proteomes:UP000076268};
RN   [1] {ECO:0000313|EMBL:KYZ77302.1, ECO:0000313|Proteomes:UP000076268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU4 {ECO:0000313|EMBL:KYZ77302.1,
RC   ECO:0000313|Proteomes:UP000076268};
RA   Choi J.K., Shah M., Yee N.;
RT   "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT   anaerobe isolated from saprolite.";
RL   Submitted (FEB-2016) 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: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:KYZ77302.1}.
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DR   EMBL; LSGP01000013; KYZ77302.1; -; Genomic_DNA.
DR   RefSeq; WP_066239395.1; NZ_LSGP01000013.1.
DR   AlphaFoldDB; A0A154BTP4; -.
DR   STRING; 1794912.AXX12_04005; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000076268; 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:KYZ77302.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:KYZ77302.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076268}.
FT   DOMAIN          49..350
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          353..452
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         274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   461 AA;  51797 MW;  AA90CEFA6639C2C4 CRC64;
     MTELTPKQIV DELNKYIVGQ HQAKRSVAIA LRNRWRSRML PSAMQEEVIP KNILMIGPTG
     VGKTEIARRL AKLVNAPFIK VEATKFTEIG YVGRDVESMV RDLVETAIRM VKQERILEVN
     DKARELADEQ IVNFFCPTVK ETPRNPFELL FSGTAGSTEP NKNDSKFDDQ AERTHWRELL
     KQGELEDELI EIAVEDITHP PMGMFAGSGM EEMGINLGDM LGNLLPKKTK KRKLTVANAR
     KILIQEEAQK LIDMDQVIAS AIQLAENAGI IFLDEIDKVA GRGRTSGPDV SREGVQRDIL
     PIVEGSTVVT KYGPVKTDHI LFIAAGAFHI SKPSDLIPEL QGRFPIRVEL TSLSKEDFRQ
     ILTEPSQALI KQYICLLAAE GVAITFSDDA VDEIANIACT INTETENIGA RRLYTVMEKL
     LEQLSYEAPD LEQKEIHIDR QYVRTMLNHI VVDQNLSHYI L
//
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