(data stored in ACNUC7421 zone)

HOGENOM: MOOTA_1_PE1002

ID   MOOTA_1_PE1002                       STANDARD;      PRT;   174 AA.
AC   MOOTA_1_PE1002; Q2RJP6;
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 subunit HslV; EC=3.4.25 2;
DE   (MOOTA_1.PE1002).
GN   Name=hslV; OrderedLocusNames=Moth_1029;
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.PE1002.
CC       Moorella thermoacetica ATCC 39073, complete genome.
CC       7874984..8874983 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:HSLV_MOOTA
CC   -!- FUNCTION: Protease subunit of a proteasome-like degradation
CC       complex believed to be a general protein degrading machinery (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with
CC       broad specificity.
CC   -!- ENZYME REGULATION: Allosterically activated by HslU binding (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 peptidase T1B family. HslV subfamily.
CC   -!- GENE_FAMILY: HOG000064533 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q2RJP6; -.
DR   EMBL; CP000232; ABC19343.1; -; Genomic_DNA.
DR   RefSeq; YP_429886.1; NC_007644.1.
DR   ProteinModelPortal; Q2RJP6; -.
DR   SMR; Q2RJP6; 3-174.
DR   STRING; Q2RJP6; -.
DR   MEROPS; T01.007; -.
DR   GeneID; 3832649; -.
DR   GenomeReviews; CP000232_GR; Moth_1029.
DR   KEGG; mta:Moth_1029; -.
DR   NMPDR; fig|264732.9.peg.1011; -.
DR   eggNOG; COG5405; -.
DR   OMA; WRTDKYL; -.
DR   PhylomeDB; Q2RJP6; -.
DR   ProtClustDB; PRK05456; -.
DR   BioCyc; MTHE264732:MOTH_1029-MON; -.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
DR   HAMAP; MF_00248; HslV; 1; -.
DR   InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR   HOGENOMDNA; MOOTA_1.PE1002; -.
KW   ATP-dependent protease peptidase subunit;
KW   Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Protease; Reference proteome; Sodium;
KW   Threonine protease.
SQ   SEQUENCE   174 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEGTTVIAVR HQGRVALAGD GQVTFGNTVM KHKARKVRRL YQDRVLAGFA GSVADAFTLF
     EKFEAKLETY HGNLQRAAVE LGKEWRTDRF LRRLEALLVV ADKEHLLIIS GNGEIVEPDD
     GIAAIGSGGP YALAAARALV AHTSMTAGEI AREAMNIAAS ICIYTNNNII VEEL
//

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