ID A3TXV3_PSEBH Unreviewed; 435 AA.
AC A3TXV3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
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=OB2597_12623 {ECO:0000313|EMBL:EAQ02987.1};
OS Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS HTCC2597) (Oceanicola batsensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ02987.1, ECO:0000313|Proteomes:UP000004318};
RN [1] {ECO:0000313|EMBL:EAQ02987.1, ECO:0000313|Proteomes:UP000004318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597
RC {ECO:0000313|Proteomes:UP000004318};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAQ02987.1}.
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DR EMBL; AAMO01000005; EAQ02987.1; -; Genomic_DNA.
DR RefSeq; WP_009806743.1; NZ_CH724131.1.
DR AlphaFoldDB; A3TXV3; -.
DR STRING; 252305.OB2597_12623; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_5; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000004318; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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:EAQ02987.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00249}; Protease {ECO:0000313|EMBL:EAQ02987.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004318}.
FT DOMAIN 49..324
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 327..426
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 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 435 AA; 48252 MW; 60A36B3947E46EBE CRC64;
MTDLTPREIV SELDRFIIGQ KDAKRAVAVA LRSRWRRRQL EDDLRDEVFP KNILMIGPTG
VGKTEISRRL AKLARAPFIK VEATKFTEVG YVGRDVEQIV RDLMDSAIAM TREHMREDVK
ATAHKMAEDR VIEALAGSDA REGTREMFRK KLRNGELDDT EIELDLADNS NPMAMLDMPG
QPGQQMGMMN LGDIFGKAFG GKTVRRKMRV ADSYEVLLGE EADKLLDDET VNRAALTAVE
ENGIVFLDEI DKVCARSDAR GAEVSREGVQ RDLLPLIEGT TVSTKYGAVR TDHILFIASG
AFHVAKPSDL LPELQGRLPI RVELQSLTEA DFVAILTETD NALTRQYTAL METEGVSVTF
TEDGIAALAK TAADVNQSVE NIGARRLYTI MERVFEELSF HAPDRTGETI SVDADFVNEN
VGKLAASADL SRYVL
//
