(data stored in SCRATCH zone)

SWISSPROT: Q3KJB5_PSEPF

ID   Q3KJB5_PSEPF            Unreviewed;       192 AA.
AC   Q3KJB5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
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=Pfl01_0397 {ECO:0000313|EMBL:ABA72141.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72141.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72141.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72141.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000094; ABA72141.1; -; Genomic_DNA.
DR   STRING; 205922.Pfl01_0397; -.
DR   EnsemblBacteria; ABA72141; ABA72141; Pfl01_0397.
DR   KEGG; pfo:Pfl01_0397; -.
DR   eggNOG; ENOG4108R5P; Bacteria.
DR   eggNOG; COG5405; LUCA.
DR   HOGENOM; HOG000064533; -.
DR   KO; K01419; -.
DR   OMA; IMKGNAR; -.
DR   Proteomes; UP000002704; Chromosome.
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; Q3KJB5.
DR   SWISS-2DPAGE; Q3KJB5.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00248};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
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, ECO:0000313|EMBL:ABA72141.1};
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, ECO:0000313|EMBL:ABA72141.1};
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     18     18       {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       173    173       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       176    176       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       179    179       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
SQ   SEQUENCE   192 AA;  20457 MW;  0718709CE34CDE1C CRC64;
     MNGHKAFSPR SVETLPLTTI VSVRRHGKVV MGGDGQVSLG NTVMKGNAKK VRRLYHGEVI
     AGFAGATADA FTLFERFEGQ LEKHQGHLVR AAVELAKEWR TDRSLSRLEA MLAVANKDAS
     LIITGNGDVV EPEDGLIAMG SGGAYAQAAA SALLKKTDLS AREIVETALG IAGDICVFTN
     HTQTIEEQDL AE
//

If you have problems or comments...

PBIL Back to PBIL home page