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Entry: A0A1A9EUU5_9GAMM
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ID   A0A1A9EUU5_9GAMM        Unreviewed;       443 AA.
AC   A0A1A9EUU5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=A8C75_01910 {ECO:0000313|EMBL:ANG61339.1};
OS   Marinobacterium aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG61339.1, ECO:0000313|Proteomes:UP000078070};
RN   [1] {ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA   Baek K., Yang S.-J.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANG61339.1, ECO:0000313|Proteomes:UP000078070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST58-10 {ECO:0000313|EMBL:ANG61339.1,
RC   ECO:0000313|Proteomes:UP000078070};
RX   PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA   Bae S.S., Jung J., Chung D., Baek K.;
RT   "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT   isolated from estuary sediment.";
RL   Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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}.
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DR   EMBL; CP015839; ANG61339.1; -; Genomic_DNA.
DR   RefSeq; WP_067377324.1; NZ_CP015839.1.
DR   AlphaFoldDB; A0A1A9EUU5; -.
DR   STRING; 1821621.A8C75_01910; -.
DR   KEGG; mars:A8C75_01910; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000078070; Chromosome.
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:UP000078070}.
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   REGION          134..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  49899 MW;  7BD05D4F2E8AB721 CRC64;
     MSNMTPREIV HELDRHIIGQ DAAKRSVAVA LRNRWRRMQL NEELRAEVSP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGRDVETIV RDLVDMAIKM VREQEMNKVR
     FRAEEAAEER ILDALLPPAR ATGNEPAPSK TDSATRQVFR KKLREHQLDD KEIELDLAQP
     KAGVEIMSPP GMEEMTSQLQ SMFANFGGDR KQHRRLPVKE AFKLLVDEEA ARMVKDEDIK
     QNAIDLVEQN GIVFLDEIDK VCKRSDSTGG DVSREGVQRD LLPLIEGCTV STKHGMVNTD
     HILFIASGAF HLARPSDLIP ELQGRLPIRV ELNALTPGDF RRILTEPNAS ITEQYRALMK
     TEGVEIEFAE DAIARIAELA FQVNEQTENI GARRLHTMME RLLEELSFTA SDLGGEKLLI
     DAAYVDKYLA ELSQDQDLSH YIL
//
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