(data stored in ACNUC7421 zone)

SWISSPROT: HSLU_RHOPS

ID   HSLU_RHOPS              Reviewed;         433 AA.
AC   Q13E33;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
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};
GN   OrderedLocusNames=RPD_0418;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex;
CC       this subunit has chaperone activity. The binding of ATP and its
CC       subsequent hydrolysis by HslU are essential for unfolding of
CC       protein substrates subsequently hydrolyzed by HslV. HslU
CC       recognizes the N-terminal part of its protein substrates and
CC       unfolds these before they are guided to HslV for hydrolysis.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on
CC       each side by a ring-shaped HslU homohexamer. The assembly of the
CC       HslU/HslV complex is dependent on binding of ATP.
CC       {ECO:0000255|HAMAP-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; CP000283; ABE37656.1; -; Genomic_DNA.
DR   RefSeq; WP_011500844.1; NC_007958.1.
DR   SMR; Q13E33; -.
DR   STRING; 316057.RPD_0418; -.
DR   PRIDE; Q13E33; -.
DR   EnsemblBacteria; ABE37656; ABE37656; RPD_0418.
DR   KEGG; rpd:RPD_0418; -.
DR   eggNOG; ENOG4105C4N; Bacteria.
DR   eggNOG; COG1220; LUCA.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   BioCyc; RPAL316057:RPD_RS02150-MONOMER; -.
DR   Proteomes; UP000001818; 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; Q13E33.
DR   SWISS-2DPAGE; Q13E33.
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Stress response.
FT   CHAIN         1    433       ATP-dependent protease ATPase subunit
FT                                HslU.
FT                                /FTId=PRO_1000012789.
FT   NP_BIND      60     65       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING      18     18       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00249}.
FT   BINDING     246    246       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING     311    311       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING     383    383       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
SQ   SEQUENCE   433 AA;  47594 MW;  7238A21A09EC8BAD CRC64;
     MTDFSPREIV SELDRFIVGQ ADAKRAVAIA LRNRWRRLQL EGILREEVLP KNILMIGPTG
     VGKTEIARRL AKLAGAPFLK VEATKFTEVG YVGRDVEQII RDLVEVAIAQ VRERKRKDVQ
     ARAQIAAEER VLDALVGPGS SPATRDSFRR KLRAGDLNDK EIEVETQASS GSPMFEIPGM
     PGGQIGAISI GDIFGKMGGR TKTRRLTVAD SHDILINEEA DKLLDNDQLV QEAINVVENN
     GIVFLDEIDK ICVRDGRSGG EVSREGVQRD LLPLIEGTTV ATKHGAVKTE HILFIASGAF
     HIAKPSDLLP ELQGRLPIRV ELNALTRDDM RRILTEPEAS LIKQYIALLQ TEGVTLEFSD
     DAIDALADVA VGVNSTVENI GARRLQTVME RVLDEISFVA PDRGGETIRI DADYVQKNVG
     DLAKNTDLSR FIL
//

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