(data stored in ACNUC30630 zone)

SWISSPROT: HSLU_RHOPT

ID   HSLU_RHOPT              Reviewed;         433 AA.
AC   B3Q8B9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 62.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249}; OrderedLocusNames=Rpal_0308;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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:0000255|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:0000255|HAMAP-
CC       Rule:MF_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
DR   EMBL; CP001096; ACE98868.1; -; Genomic_DNA.
DR   RefSeq; WP_012494055.1; NC_011004.1.
DR   SMR; B3Q8B9; -.
DR   PRIDE; B3Q8B9; -.
DR   EnsemblBacteria; ACE98868; ACE98868; Rpal_0308.
DR   KEGG; rpt:Rpal_0308; -.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   BioCyc; RPAL395960:RPAL_RS01545-MONOMER; -.
DR   Proteomes; UP000001725; Chromosome.
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:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR43815; PTHR43815; 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; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   3: Inferred from homology;
DR   PRODOM; B3Q8B9.
DR   SWISS-2DPAGE; B3Q8B9.
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..433
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000100967"
FT   NP_BIND         60..65
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         18
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         246
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         311
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         383
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   433 AA;  47460 MW;  4B1D655AC5E073D1 CRC64;
     MTDFSPREIV SELDRFIVGQ ADAKRAVAIA LRNRWRRLQL EGSLREEVLP KNILMIGPTG
     VGKTEIARRL AKLAGAPFLK VEATKFTEVG YVGRDVEQII RDLVEVAIAQ VREKKRKDVQ
     ARAQVAAEER VLDALVGPGS GPATRDSFRK KLRAGELNDK EIEIETQAGS GSPMFEIPGM
     PGAQIGAVSL GDIFGKMGGR TKKRRLTVAD SHEILVNEEA DKLLDTDQLV QEAIAAVENN
     GIVFLDEIDK ICVRDGRSGG EVSREGVQRD LLPLIEGTTV STKHGAVKTE HILFIASGAF
     HIAKPSDLLP ELQGRLPIRV ELNALSRDDM RRILTEPEAS LIKQYVALMK TEGVTLDFSD
     DAIDALADVA VAVNSTVENI GARRLQTVME RVLDEISFVA PDRHGETFQV DADYVKTNVG
     DLAKNTDLSR FIL
//

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