(data stored in SCRATCH zone)

SWISSPROT: D3VH23_XENNA

ID   D3VH23_XENNA            Unreviewed;       176 AA.
AC   D3VH23;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 57.
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   ECO:0000313|EMBL:CBJ88308.1};
GN   OrderedLocusNames=XNC1_0220 {ECO:0000313|EMBL:CBJ88308.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88308.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88308.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88308.1; -; Genomic_DNA.
DR   RefSeq; WP_010847670.1; NC_014228.1.
DR   STRING; 406817.XNC1_0220; -.
DR   MEROPS; T01.006; -.
DR   EnsemblBacteria; CBJ88308; CBJ88308; XNC1_0220.
DR   KEGG; xne:XNC1_0220; -.
DR   eggNOG; ENOG4108R5P; Bacteria.
DR   eggNOG; COG5405; LUCA.
DR   HOGENOM; HOG000064533; -.
DR   KO; K01419; -.
DR   OMA; IMKGNAR; -.
DR   Proteomes; UP000008075; 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; D3VH23.
DR   SWISS-2DPAGE; D3VH23.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00248};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
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:CBJ88308.1};
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:CBJ88308.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
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      2      2       {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       157    157       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       160    160       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
FT   METAL       163    163       Sodium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00248}.
SQ   SEQUENCE   176 AA;  19101 MW;  68E44A2EAE0AD1A4 CRC64;
     MTTIVSVRRN GKVVIGGDGQ ATMGHTVMKG NVRKVRRLYN DKVIAGFAGG TADAFTLFEL
     FERKLEMHQG HLTKAAVELA KDWRTDRMLR KLEALLAVAD ENASLIITGN GDVIQPENDL
     IAIGSGGSYA QAAARAMLET TDLGAREITE RALSIAADIC IYTNHNHNFE ELSSKA
//

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