(data stored in SCRATCH zone)

SWISSPROT: Q4ZZF7_PSEU2

ID   Q4ZZF7_PSEU2            Unreviewed;       192 AA.
AC   Q4ZZF7;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
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=Psyr_0395 {ECO:0000313|EMBL:AAY35465.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35465.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35465.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35465.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35465.1; -; Genomic_DNA.
DR   RefSeq; YP_233503.2; NC_007005.1.
DR   STRING; 205918.Psyr_0395; -.
DR   EnsemblBacteria; AAY35465; AAY35465; Psyr_0395.
DR   GeneID; 3365871; -.
DR   KEGG; psb:Psyr_0395; -.
DR   PATRIC; fig|205918.7.peg.409; -.
DR   eggNOG; ENOG4108R5P; Bacteria.
DR   eggNOG; COG5405; LUCA.
DR   HOGENOM; HOG000064533; -.
DR   KO; K01419; -.
DR   OMA; IMKGNAR; -.
DR   Proteomes; UP000000426; 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; Q4ZZF7.
DR   SWISS-2DPAGE; Q4ZZF7.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00248};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
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   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;  20420 MW;  50A18C4B0CE441AA CRC64;
     MSLHQGIFAP QCGDSPLTTI VSVRRHGKVV MAGDGQVSLG NTVMKGNAKK VRRLYHGEVI
     AGFAGATADA FTLFERFEAQ LEKHQGHLVR AAVELAKDWR TDRSLSRLEA MLAVANKDAS
     LIITGNGDVV EPEDGLIAMG SGGAFAQAAA RALLLKTDLS AREIAETSLH IAGDICVFTN
     HNITIEEQDL AG
//

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