(data stored in ACNUC9543 zone)

SWISSPROT: HSLU_YERPA

ID   HSLU_YERPA              Reviewed;         443 AA.
AC   Q1CBE8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=YPA_0255;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12224.1; -; Genomic_DNA.
DR   RefSeq; WP_002208943.1; NZ_CP009906.1.
DR   SMR; Q1CBE8; -.
DR   PRIDE; Q1CBE8; -.
DR   EnsemblBacteria; ABG12224; ABG12224; YPA_0255.
DR   KEGG; ypa:YPA_0255; -.
DR   HOGENOM; HOG000010036; -.
DR   KO; K03667; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000001971; 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; Q1CBE8.
DR   SWISS-2DPAGE; Q1CBE8.
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Stress response.
FT   CHAIN         1    443       ATP-dependent protease ATPase subunit
FT                                HslU.
FT                                /FTId=PRO_1000012833.
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     256    256       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING     321    321       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
FT   BINDING     393    393       ATP. {ECO:0000255|HAMAP-Rule:MF_00249}.
SQ   SEQUENCE   443 AA;  49804 MW;  C8F480057C17E789 CRC64;
     MSEMTPREIV SELDSHIIGQ DKAKRAVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRHQSIEKMR
     YRAEELAEER ILDVLIPPAK NNWGVPDESQ EPSATRQTFR KKLREGQLDD KEIEIDLAAA
     PMGVEIMAPP GMEEMTNQLQ SMFQNIAGQK QKPRKIKIKE ALKLLIEEEA AKLVNPEELK
     QQAIDAVEQH GIVFIDEIDK ICKRGQTSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
     HILFIASGAF QVSSPSDLIP ELQGRLPIRV ELQALTTDDF ERILTEPSAS LTEQYKALMA
     TEGVTIEFTR EGIRKIAEAA WQVNERTENI GARRLHTVLE RLMEDISYDA SESSGQSITI
     DAEYVGKHLD ELVADEDLSR FIL
//

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