(data stored in SCRATCH zone)

SWISSPROT: D1CEM1_THET1

ID   D1CEM1_THET1            Unreviewed;       185 AA.
AC   D1CEM1;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=ATP-dependent protease subunit HslV {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00019556};
DE            EC=3.4.25.2 {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347012};
GN   Name=hslV {ECO:0000256|HAMAP-Rule:MF_00248};
GN   OrderedLocusNames=Tter_0456 {ECO:0000313|EMBL:ACZ41377.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41377.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41377.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Protease subunit of a proteasome-like degradation
CC       complex believed to be a general protein degrading machinery.
CC       {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347025}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent cleavage of peptide bonds with broad
CC         specificity.; EC=3.4.25.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00248, ECO:0000256|SAAS:SAAS01118573};
CC   -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS01071303}.
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:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248,
CC       ECO:0000256|SAAS:SAAS00347051}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00542229}.
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DR   EMBL; CP001825; ACZ41377.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0456; -.
DR   MEROPS; T01.007; -.
DR   EnsemblBacteria; ACZ41377; ACZ41377; Tter_0456.
DR   KEGG; ttr:Tter_0456; -.
DR   eggNOG; ENOG4108R5P; Bacteria.
DR   eggNOG; COG5405; LUCA.
DR   HOGENOM; HOG000064533; -.
DR   KO; K01419; -.
DR   OMA; IMKGNAR; -.
DR   BioCyc; TTER525904:G1GGS-461-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
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   CDD; cd01913; protease_HslV; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00248; HslV; 1.
DR   InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; PTHR32194; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PIRSF; PIRSF039093; HslV; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CEM1.
DR   SWISS-2DPAGE; D1CEM1.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00248};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248,
KW   ECO:0000256|SAAS:SAAS00425220};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00248,
KW   ECO:0000256|SAAS:SAAS00425230};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00248,
KW   ECO:0000256|SAAS:SAAS00019499};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00248,
KW   ECO:0000256|SAAS:SAAS00425208};
KW   Proteasome {ECO:0000313|EMBL:ACZ41377.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Sodium {ECO:0000256|HAMAP-Rule:MF_00248,
KW   ECO:0000256|SAAS:SAAS00425233};
KW   Threonine protease {ECO:0000256|HAMAP-Rule:MF_00248,
KW   ECO:0000256|SAAS:SAAS00425169}.
FT   ACT_SITE     11     11       {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       166    166       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       169    169       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       172    172       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
SQ   SEQUENCE   185 AA;  20242 MW;  2F9186A5D46AE217 CRC64;
     MSHNPPMMRA TTILAVLRDG LLAMAGDGQV TFGDSIFKHK ARKVRTLYDG KVLVGFAGAV
     ADALTLFERF ESQLQQYSGD LRRSAVELAK QWRTDRYLRP LEAELIVGDP GQLLLITGQG
     EVIEPDEGIL AIGSGSVYAL AAAQALLRHT NMDAEHITLE AMKIAAELCI YTNDNITIET
     IRAEN
//

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