(data stored in ACNUC19708 zone)

HOGENOM: ACEP3_1_PE1015

ID   ACEP3_1_PE1015                       STANDARD;      PRT;   437 AA.
AC   ACEP3_1_PE1015; C7JGG4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Endopeptidase ATP-dependent hsl ATP-binding subunit HslU;
DE   (ACEP3_1.PE1015).
GN   Name=hslU; OrderedLocusNames=APA01_10240;
OS   ACETOBACTER PASTEURIANUS IFO 3283-01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=634452;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACEP3_1.PE1015.
CC       Acetobacter pasteurianus IFO 3283-01, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7JGG4_ACEP3
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 (By
CC       similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- GENE_FAMILY: HOG000010036 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C7JGG4; -.
DR   EMBL; AP011121; BAH99173.1; -; Genomic_DNA.
DR   RefSeq; YP_003187553.1; NC_013209.1.
DR   STRING; C7JGG4; -.
DR   GeneID; 8436690; -.
DR   GenomeReviews; AP011121_GR; APA01_10240.
DR   KEGG; apt:APA01_10240; -.
DR   OMA; EASKFTE; -.
DR   ProtClustDB; PRK05201; -.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   PANTHER; PTHR11262:SF3; 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   TIGRFAMs; TIGR00390; HslU; 1.
DR   HOGENOMDNA; ACEP3_1.PE1015; -.
KW   ATP-dependent protease ATP-binding subunit HslU;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding.
SQ   SEQUENCE   437 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDAPNFSPRE IVSELDRFIV GQQDAKRAVA IAMRNRWRRA QLSEGMREEV VPKNILMIGP
     TGCGKTEIAR RLAKLAQAPF LKVEATKFTE VGYVGRDVDS IVRDLVEVSI TMLKTSRRKD
     VEEKARQAAE ERIIDALAGE GSSADTKSKF RSMLRSGQLE DKEIDIAVTE QAPAGSSDMP
     GAVPGQAINV GDMMKAFMNR GPKQKKLKVS VAREYLKREE ADRLLDGEAL TREAVANAQE
     NGIVFLDEID KVCARASESG AKGGDVSREG VQRDLLPLIE GTTVSTKHGP VNTDHILFIA
     SGAFHLAKPS DLLPELQGRL PIRVELQPLS REDLRRILTD PEHSLLKQYI ALMGTEGVTL
     NFTDDAIDAL AELAADINDR VENIGARRLA TVLERLLEEV SFTASDRKGE TVEVNAAMVQ
     EKVAPLARKG DLSRFIL
//

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