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Database: UniProt
Entry: H5TEJ4_9ALTE
LinkDB: H5TEJ4_9ALTE
Original site: H5TEJ4_9ALTE 
ID   H5TEJ4_9ALTE            Unreviewed;       442 AA.
AC   H5TEJ4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-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   ECO:0000313|EMBL:GAB56721.1};
GN   ORFNames=GPUN_2606 {ECO:0000313|EMBL:GAB56721.1};
OS   Glaciecola punicea ACAM 611.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB56721.1, ECO:0000313|Proteomes:UP000053586};
RN   [1] {ECO:0000313|EMBL:GAB56721.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56721.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=22628500; DOI=10.1128/JB.00463-12;
RA   Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA   Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT   "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT   punicea ACAM 611T.";
RL   J. Bacteriol. 194:3267-3267(2012).
RN   [2] {ECO:0000313|EMBL:GAB56721.1, ECO:0000313|Proteomes:UP000053586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB56721.1,
RC   ECO:0000313|Proteomes:UP000053586};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAB56721.1}.
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DR   EMBL; BAET01000031; GAB56721.1; -; Genomic_DNA.
DR   RefSeq; WP_006007177.1; NZ_BAET01000031.1.
DR   AlphaFoldDB; H5TEJ4; -.
DR   STRING; 56804.BAE46_04555; -.
DR   eggNOG; COG1220; Bacteria.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000053586; 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:GAB56721.1};
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:GAB56721.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:GAB56721.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053586}.
FT   DOMAIN          49..331
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          334..430
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         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;  49226 MW;  6C76204D6C81F1CB CRC64;
     MSEMTPREIV HALDKHIIGQ ADAKRAVSIA LRNRWRRMQL EPELRQEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVESII RDLADIAVKM TKESAAVKVR
     HRAEEAAEER ILDILIPPAE SPSGEKAPAE DRGARQVFRK KLREGTLDDK EIEISVSLPQ
     VGVEIMAPPG MEEMTNQLQG MFQNLSGDKK KKKRLKIKDA FKLLVEEESA KLINNEDLKE
     NAIESLEQTG IVFIDEIDKI CKSGNNSGAD ISREGVQRDL LPLVEGSTVS TKHGMVKTDH
     ILFIASGAFQ MSKPSDLIPE LQGRLPIRVE LSALTTGDFV RILTEPKASL TEQYKALLAT
     EGVGVTFDES GIKRIAEAAW QVNERTENIG ARRLHTVLER LMEDISFEAS DKSGESYIID
     ESYVNEHLQA LVDNEDLSRF IL
//
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