(data stored in ACNUC7421 zone)

HOGENOM: MOOTA_1_PE1003

ID   MOOTA_1_PE1003                       STANDARD;      PRT;   461 AA.
AC   MOOTA_1_PE1003; Q2RJP5;
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   RecName: Full=ATP-dependent protease ATPase subunit HslU;AltName:
DE   Full=Unfoldase HslU; (MOOTA_1.PE1003).
GN   Name=hslU; OrderedLocusNames=Moth_1030;
OS   MOORELLA THERMOACETICA ATCC 39073.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOOTA_1.PE1003.
CC       Moorella thermoacetica ATCC 39073, complete genome.
CC       7874984..8874983 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q2RJP5_MOOTA
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   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC   -!- GENE_FAMILY: HOG000010036 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q2RJP5; -.
DR   EMBL; CP000232; ABC19344.1; -; Genomic_DNA.
DR   RefSeq; YP_429887.1; NC_007644.1.
DR   ProteinModelPortal; Q2RJP5; -.
DR   SMR; Q2RJP5; 2-134.
DR   STRING; Q2RJP5; -.
DR   GeneID; 3832650; -.
DR   GenomeReviews; CP000232_GR; Moth_1030.
DR   KEGG; mta:Moth_1030; -.
DR   NMPDR; fig|264732.9.peg.1012; -.
DR   eggNOG; COG1220; -.
DR   OMA; EASKFTE; -.
DR   PhylomeDB; Q2RJP5; -.
DR   ProtClustDB; PRK05201; -.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:HAMAP.
DR   GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
DR   GO; GO:0043335; P:protein unfolding; IEA:HAMAP.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   HAMAP; MF_00249; HslU; 1; -.
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; MOOTA_1.PE1003; -.
KW   ATP-dependent protease ATP-binding subunit HslU;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Reference proteome; Stress response.
SQ   SEQUENCE   461 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDFTPRQIVA ELDRYIIGQE EAKKCVAVAL RNRYRRQKLN PELRDEVLPK NIIMIGPTGV
     GKTEIARRLA KLVGAPFLKV EATRFTEVGY VGRDVESMIR ELVENAVRMV KIEKRAEVEA
     KAAKMAEKRL LDLLVPRQGK EKGTHNPWEV LFGGAQVNSE GTVLEEESLR EKRAILREKL
     RRQELEDMMV EVEVEDTTGP GGVILGGLGL EELGINLQDM LGNMLPRRKR KRLVTVAEAR
     RILTQQEADK LIDMDDVAAI AVQRVEQEGI IFLDEIDKIA GRESSHGPDV SREGVQRDIL
     PIVEGTTVQT KYGPVKTDHI LFIAAGAFHV AKPADLIPEL QGRFPLRVEL KSLGREDFQR
     ILTEPKNSLL KQYTALLAVD GIELQFSADA IAEIADIAYT VNTQGEDIGA RRLHTILEKI
     LQDLLFEAPE VQERKVVIDR TYVRKQLGDI MQRTDVQAYI L
//

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