ID K2JP60_9GAMM Unreviewed; 443 AA.
AC K2JP60;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=B3C1_02520 {ECO:0000313|EMBL:EKE77043.1};
OS Gallaecimonas xiamenensis 3-C-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE77043.1, ECO:0000313|Proteomes:UP000006755};
RN [1] {ECO:0000313|EMBL:EKE77043.1, ECO:0000313|Proteomes:UP000006755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-C-1 {ECO:0000313|EMBL:EKE77043.1,
RC ECO:0000313|Proteomes:UP000006755};
RX PubMed=23209203; DOI=10.1128/JB.01854-12;
RA Lai Q., Wang L., Wang W., Shao Z.;
RT "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL J. Bacteriol. 194:6937-6937(2012).
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:EKE77043.1}.
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DR EMBL; AMRI01000003; EKE77043.1; -; Genomic_DNA.
DR RefSeq; WP_008482696.1; NZ_AMRI01000003.1.
DR AlphaFoldDB; K2JP60; -.
DR STRING; 745411.B3C1_02520; -.
DR PATRIC; fig|745411.4.peg.494; -.
DR eggNOG; COG1220; Bacteria.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000006755; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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:UP000006755};
KW Stress response {ECO:0000313|EMBL:EKE77043.1}.
FT DOMAIN 49..332
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 335..429
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 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 443 AA; 49821 MW; 1A78D952CD5722CA CRC64;
MSSMTPREIV HELDRHIIGQ ANAKRSVAIA LRNRWRRMQL DEALRQEVTP KNILMIGPTG
VGKTEIARRL ARLANAPFIK VEATKFTEVG YVGKEVEQII RDLADVAMKM TREQEMKKVR
TRAEEAAEER ILDALLPRPR NQWGESEKAE GDNHTRQVFR KKLREGSLDD KEIDIDIAAP
QMDMQIMAPP GMEEMTNQLQ SMFQNLGGQT KQSKKLKVKD ALKLAIDEEA AKLLNPEEVK
EKALAAVENN GIVFLDEIDK ICKRGDTSGP DVSREGVQRD LLPLVEGCTV NTKHGMVKTD
HILFIASGAF QMAKPSDLIP ELQGRLPIRV ELDALTAEDF VRILTEPKAS LTEQYKALMA
TEGVKVEFTE DGIHKLAEAA WQVNERTENI GARRLHTVME RMMEDISFAA ADHDGETLTI
DAAYVQSHLG KLVEDEDLSR FIL
//
