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Database: UniProt
Entry: A0A0F4PTL6_9GAMM
LinkDB: A0A0F4PTL6_9GAMM
Original site: A0A0F4PTL6_9GAMM 
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
//
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