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
//