ID A0A5B2Z8W7_9GAMM Unreviewed; 445 AA.
AC A0A5B2Z8W7;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:KAA2284596.1};
GN ORFNames=F0415_07790 {ECO:0000313|EMBL:KAA2284596.1};
OS Arenimonas fontis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=2608255 {ECO:0000313|EMBL:KAA2284596.1, ECO:0000313|Proteomes:UP000322165};
RN [1] {ECO:0000313|EMBL:KAA2284596.1, ECO:0000313|Proteomes:UP000322165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3729k {ECO:0000313|EMBL:KAA2284596.1,
RC ECO:0000313|Proteomes:UP000322165};
RA Zayulina K.S., Prokofeva M.I., Elcheninov A.G., Novikov A.,
RA Kochetkova T.V., Kublanov I.V.;
RT "Arenimonas chukotkensis sp. nov., a bacterium isolated from Chukotka hot
RT spring, Arctic region, Russia.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA2284596.1, ECO:0000313|Proteomes:UP000322165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3729k {ECO:0000313|EMBL:KAA2284596.1,
RC ECO:0000313|Proteomes:UP000322165};
RA Mazur A.;
RL Submitted (SEP-2019) 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:KAA2284596.1}.
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DR EMBL; VUOD01000005; KAA2284596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B2Z8W7; -.
DR Proteomes; UP000322165; 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 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:KAA2284596.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:KAA2284596.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000322165}.
FT DOMAIN 49..334
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 337..431
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 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 445 AA; 49731 MW; EF769A05CB3A2E98 CRC64;
MTQLTPREIV GELDRYIVGQ AAAKRAVAIA LRNRWRRMQL EPGMRDEVMP KNILMIGPTG
VGKTEIARRL AALANAPFVK VEATRFTEVG YVGKDVEQII RDLAEVAVKM FREQAKQRVR
TQAEERAEDR ILEALLPKRR GPGFMVEVAP DGEDGTRAKL RRQLRAGELD EREIELELAQ
LGAGLDIMTP PGMEEMGQQL RQMFQNLGGG RASRRHLTVK AARPLLIEEE AGKLVNEEEI
RTQALEACEQ NGIVFIDEID KVARRKDVVG GADVSREGVQ RDLLPLVEGS TVNTRYGPVK
TDHILFIASG AFHLSKPSDL IPELQGRFPI RVELDALGRE DFKRILTEPK NALVRQYTAL
LATEGVNIGF DAEAIDRLAE IAFLINERQE NIGARRLHTV LEKLLEKLSF EAPDKGGLSL
MVDRAMVDEQ LGDAVQDPDL SRYIL
//