ID A0A0F4PTL6_9GAMM Unreviewed; 442 AA.
AC A0A0F4PTL6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:KJY98777.1};
GN ORFNames=CWC05_18655 {ECO:0000313|EMBL:TMP85455.1}, TW72_13775
GN {ECO:0000313|EMBL:KJY98777.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY98777.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJY98777.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJY98777.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
RN [2] {ECO:0000313|EMBL:TMP85455.1, ECO:0000313|Proteomes:UP000305874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2897 {ECO:0000313|EMBL:TMP85455.1,
RC ECO:0000313|Proteomes:UP000305874};
RA Paulsen S., Gram L.K.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000305874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2897 {ECO:0000313|Proteomes:UP000305874};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:TMP85455.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S2897 {ECO:0000313|EMBL:TMP85455.1};
RA Sonnenschein E.C., Bech P.K.;
RT "Co-occurence of chitin degradation, pigmentation and bioactivity in marine
RT Pseudoalteromonas.";
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:KJY98777.1}.
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DR EMBL; JXXZ01000010; KJY98777.1; -; Genomic_DNA.
DR EMBL; PNCG01000029; TMP85455.1; -; Genomic_DNA.
DR RefSeq; WP_022946650.1; NZ_PPSV01000010.1.
DR AlphaFoldDB; A0A0F4PTL6; -.
DR STRING; 151081.TW72_13775; -.
DR GeneID; 58229564; -.
DR PATRIC; fig|151081.8.peg.3426; -.
DR eggNOG; COG1220; Bacteria.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000033664; Unassembled WGS sequence.
DR Proteomes; UP000305874; 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; 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:KJY98777.1};
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:KJY98777.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:KJY98777.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033664}.
FT DOMAIN 49..331
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 334..428
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 137..163
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 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 442 AA; 49624 MW; 2C0B73EB828847D5 CRC64;
MSAMTPREIV HELDQHIIGQ SNAKKAVAIA LRNRWRRMQL DESLRPEVTP KNILMIGPTG
VGKTEIARRL AKLANAPFLK VEATKFTEVG YVGKEVETII RDLVDIAIKM VREQQAKKHH
FRAEEAAEER ILDALLPPAK DTWGESQPSE NSSTRQSFRK KLREGQLDDK EIEIDVAEQA
PNVEIMSPPG MEEMTNQLQS MFQNMSGGKT KKRKLKIKEA FKLLVEEEAA KLVNPEDVKE
LAIEAVEQHG IVFLDEVDKI CKRGEANGPD VSREGVQRDL LPLIEGSSVS TKHGMVKTDH
ILFIASGAFQ MAKPSDLIPE LQGRLPIRVE LDALSADDFK RILTEPHASL TEQQIALMNT
EEVTIEFTDD AIDSIAQAAW QVNEKTENIG ARRLHTVMER LMEEISFDAS DKAGSRLTID
GEYVNQHLGN LVQDEDLSRF IL
//