(data stored in SCRATCH3701 zone)

SWISSPROT: HSLV_RICTY

ID   HSLV_RICTY              Reviewed;         182 AA.
AC   Q68X53;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 83.
DE   RecName: Full=ATP-dependent protease subunit HslV {ECO:0000255|HAMAP-Rule:MF_00248};
DE            EC=3.4.25.2 {ECO:0000255|HAMAP-Rule:MF_00248};
GN   Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248}; OrderedLocusNames=RT0309;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Protease subunit of a proteasome-like degradation complex
CC       believed to be a general protein degrading machinery.
CC       {ECO:0000255|HAMAP-Rule:MF_00248}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent cleavage of peptide bonds with broad
CC         specificity.; EC=3.4.25.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00248};
CC   -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
CC       {ECO:0000255|HAMAP-Rule:MF_00248}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on each
CC       side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV
CC       complex is dependent on binding of ATP. {ECO:0000255|HAMAP-
CC       Rule:MF_00248}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00248}.
DR   EMBL; AE017197; AAU03789.1; -; Genomic_DNA.
DR   RefSeq; WP_011190773.1; NC_006142.1.
DR   SMR; Q68X53; -.
DR   STRING; 257363.RT0309; -.
DR   EnsemblBacteria; AAU03789; AAU03789; RT0309.
DR   KEGG; rty:RT0309; -.
DR   eggNOG; ENOG4108R5P; Bacteria.
DR   eggNOG; COG5405; LUCA.
DR   HOGENOM; HOG000064533; -.
DR   KO; K01419; -.
DR   OMA; IMKGNAR; -.
DR   OrthoDB; 1129370at2; -.
DR   BioCyc; RTYP257363:G1G0L-315-MONOMER; -.
DR   Proteomes; UP000000604; 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; Q68X53.
DR   SWISS-2DPAGE; Q68X53.
KW   Allosteric enzyme; Cytoplasm; Hydrolase; Metal-binding; Protease; Sodium;
KW   Threonine protease.
FT   CHAIN           1..182
FT                   /note="ATP-dependent protease subunit HslV"
FT                   /id="PRO_0000148141"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   METAL           166
FT                   /note="Sodium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   METAL           169
FT                   /note="Sodium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   METAL           172
FT                   /note="Sodium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
SQ   SEQUENCE   182 AA;  19839 MW;  4B456657A3D85475 CRC64;
     MSDNLALHGT TILCLKKNEE IIIAADGQVS HGNTVLKSTA RKLRTIANNK IIVGFAGSTA
     DGLALFEKLE IKIEQYNSNL LRSAVELAKD WRNDKYLRRL EAMMIVADRS HILILTGNGD
     VIEPENNIAA IGSGGLFALS AARALMSYEN NLTAEEIALK SMNIAADLCV FSNHNIIMEK
     VV
//

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