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Database: UniProt
Entry: A0A656HJB8_THINJ
LinkDB: A0A656HJB8_THINJ
Original site: A0A656HJB8_THINJ 
ID   A0A656HJB8_THINJ        Unreviewed;       455 AA.
AC   A0A656HJB8;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   13-SEP-2023, entry version 14.
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=Thini_2792 {ECO:0000313|EMBL:EIJ35329.1};
OS   Thiothrix nivea (strain ATCC 35100 / DSM 5205 / JP2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=870187 {ECO:0000313|EMBL:EIJ35329.1, ECO:0000313|Proteomes:UP000005317};
RN   [1] {ECO:0000313|Proteomes:UP000005317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35100 / DSM 5205 / JP2
RC   {ECO:0000313|Proteomes:UP000005317};
RX   PubMed=22675589; DOI=10.4056/sigs.2344929;
RA   Lapidus A., Nolan M., Lucas S., Glavina Del Rio T., Tice H., Cheng J.F.,
RA   Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., Pagani I.,
RA   Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Brambilla E.M., Rohde M., Abt B., Verbarg S.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Genome sequence of the filamentous, gliding Thiothrix nivea neotype strain
RT   (JP2(T)).";
RL   Stand. Genomic Sci. 5:398-406(2011).
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; JH651384; EIJ35329.1; -; Genomic_DNA.
DR   RefSeq; WP_002709235.1; NZ_JH651384.1.
DR   AlphaFoldDB; A0A656HJB8; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000005317; 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   Pfam; PF10431; ClpB_D2-small; 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:EIJ35329.1};
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:EIJ35329.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:EIJ35329.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005317}.
FT   DOMAIN          51..349
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          348..446
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          144..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         62..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   455 AA;  51311 MW;  DF43328E47BCE8F8 CRC64;
     MPVATMTPRE IVQELDKHVI GQDKAKRSVA IALRNRWRRQ QLDETLRHEV TPKNILMIGP
     TGVGKTEIAR RLAKLANAPF IKVEATKFTE VGYVGKEVDS IIRDLADMAM KMMREQEVAK
     VNYRAQEAAA ERILDILLPA PRKETPTNEW LSNGDEEPAK PAREDSATRQ KFRKKLREGE
     LDDKEIELDV AVGGASVEIM TPPGMEEMAS QLQSMFQNIG SNKKRKRKMK IKDALKVLTE
     EEAHKMVNEE ELKQRALFAV EQTGIVFLDE IDKVARSGQT SGADVSREGV QRDLLPLIEG
     CTVNTKYGMV KTDHILFIAS GAFHVSKPSD LIPELQGRLP IRVEMDALSA NDFERILTEP
     NASLTEQYEG LLKTEGVELH FTPDAIRRIA EIAFEVNERT ENIGARRLHT VVERLLENVL
     FDAPDCDNQM TVDAEYVNNT LGELVKDEDL SRYIL
//
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