GenomeNet

Database: UniProt
Entry: A0A327NFX0_9BACT
LinkDB: A0A327NFX0_9BACT
Original site: A0A327NFX0_9BACT 
ID   A0A327NFX0_9BACT        Unreviewed;       461 AA.
AC   A0A327NFX0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=HMF3257_07790 {ECO:0000313|EMBL:RAI74250.1};
OS   Spirosoma telluris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=2183553 {ECO:0000313|EMBL:RAI74250.1, ECO:0000313|Proteomes:UP000249016};
RN   [1] {ECO:0000313|EMBL:RAI74250.1, ECO:0000313|Proteomes:UP000249016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF3257 {ECO:0000313|EMBL:RAI74250.1,
RC   ECO:0000313|Proteomes:UP000249016};
RA   Kang H., Cha I., Kim H., Kang J., Joh K.;
RT   "Spirosoma sp. HMF3257 Genome sequencing and assembly.";
RL   Submitted (JUN-2018) 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:RAI74250.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QLII01000001; RAI74250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327NFX0; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000249016; 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: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; 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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249016}.
FT   DOMAIN          53..348
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          351..444
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         64..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         409
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   461 AA;  51419 MW;  778658A09334F495 CRC64;
     MTHLLKDLTP RQIVAELDQY IIGQKDAKRN VAIALRNRWR RMNSPADMQR EITPNNILMI
     GATGVGKTEI ARRLAKLADA PFIKVEASKF TEVGYVGRDV ESMVRDLVEQ AVNMVRASKK
     EAVQAKAQQL VEDAILDILI PPVKPANGQL GFENEKKDAD AELNERTRER FREKIRSGEM
     DDRKIDIDVQ QSQTPNIGIM GGSVDDLSMM NIQEMIGGMM PKRGKKRKVS IAEARKILLE
     EEAAKLIDMD EVKEEAIRKA EDAGIIFIDE IDKVASARSG NGGGGPDVSR EGVQRDLLPI
     VEGSAVNTKY GVIHTDHILF IAAGAFHVAK PSDLIPELQG RFPIRVELQS LSEDDFYQIL
     KEPKNALTKQ YEAMLQAENV GLTFQDDALR ELARIAFEVN SDVENIGARR LQTVLSHLMN
     DFMFDIPDVI GANAQVVITK ELVSERLNGL VKNRDLSQFI L
//
DBGET integrated database retrieval system