ID I5C1J0_9BACT Unreviewed; 471 AA.
AC I5C1J0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ECO:0000313|EMBL:EIM75692.1};
GN ORFNames=A3SI_12624 {ECO:0000313|EMBL:EIM75692.1};
OS Nitritalea halalkaliphila LW7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Nitritalea.
OX NCBI_TaxID=1189621 {ECO:0000313|EMBL:EIM75692.1, ECO:0000313|Proteomes:UP000005551};
RN [1] {ECO:0000313|EMBL:EIM75692.1, ECO:0000313|Proteomes:UP000005551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW7 {ECO:0000313|EMBL:EIM75692.1,
RC ECO:0000313|Proteomes:UP000005551};
RA Jangir P.K., Singh A., Shivaji S., Sharma R.;
RT "Genome sequence of Nitritalea halalkaliphila LW7.";
RL Submitted (MAY-2012) 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:EIM75692.1}.
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DR EMBL; AJYA01000028; EIM75692.1; -; Genomic_DNA.
DR RefSeq; WP_009055663.1; NZ_AJYA01000028.1.
DR AlphaFoldDB; I5C1J0; -.
DR STRING; 1189621.A3SI_12624; -.
DR PATRIC; fig|1189621.3.peg.2635; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000005551; 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, ECO:0000313|EMBL:EIM75692.1};
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:EIM75692.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:EIM75692.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005551}.
FT DOMAIN 53..358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 361..457
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 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 471 AA; 53156 MW; 82945D2AA21BFD03 CRC64;
MKNEFDYLTP RQIVAELDKY IIGQQDAKRN VAIALRNRIR RLKVKEEIQR DIVPNNILMI
GSTGVGKTEI ARRLAKVAQA PFTKVEASKF TEVGYVGRDV ESMVRDLVEQ AIHVVREKKN
EEVKEKAAEA VEEQILDILI PPVKKAGFAP NFSRQNQVDT EFNPEQADSE ELNERTRERF
REKLRNGDLE ERKIEITVKQ SPSVGVGMIG NGMMDDASMA GLQDMLSGMM PKKTKKRKLS
ISEARKVLME EETSKLIDMD DLKEEAIRLA ENNGIIFIDE IDKIASKSSK MGGGGPDVSR
EGVQRDLLPI VEGSAVNTKY GIVHTDHVLF IAAGAFHVSK PSDLIPELQG RFPIRVELQS
LTEGDFYKIL KEPKNALTKQ YEALFGAEEV HLEFTDDAIK EIARLAYTLN EEVENIGARR
LHTVMSHLLN DFLFDVPDTI TPHARLMITA EMVQERLSSL VTNRDLSQYI L
//
