ID   HSLV_EHRRW              Reviewed;         189 AA.
AC   Q5HAB3; Q5FDM7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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};
GN   OrderedLocusNames=Erum7680, ERWE_CDS_08110;
OS   Ehrlichia ruminantium (strain Welgevonden).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=254945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA   Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA   Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA   Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA   Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA   Allsopp B.A.;
RT   "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT   tandem repeats of actively variable copy number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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}.
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DR   EMBL; CR767821; CAH58502.1; -; Genomic_DNA.
DR   EMBL; CR925678; CAI27305.1; -; Genomic_DNA.
DR   RefSeq; WP_011155447.1; NC_006832.1.
DR   AlphaFoldDB; Q5HAB3; -.
DR   SMR; Q5HAB3; -.
DR   STRING; 254945.Erum7680; -.
DR   MEROPS; T01.006; -.
DR   EnsemblBacteria; CAI27305; CAI27305; ERWE_CDS_08110.
DR   GeneID; 56785543; -.
DR   KEGG; eru:Erum7680; -.
DR   KEGG; erw:ERWE_CDS_08110; -.
DR   eggNOG; COG5405; Bacteria.
DR   HOGENOM; CLU_093872_1_0_5; -.
DR   OMA; IMKGNAR; -.
DR   BioCyc; ERUM254945:ERUM_RS04155-MON; -.
DR   Proteomes; UP000001021; 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 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;
KW   Allosteric enzyme; Cytoplasm; Hydrolase; Metal-binding; Protease; Sodium;
KW   Threonine protease.
FT   CHAIN           1..189
FT                   /note="ATP-dependent protease subunit HslV"
FT                   /id="PRO_1000012611"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         172
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         175
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         178
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
SQ   SEQUENCE   189 AA;  20727 MW;  4E2AF3CAC3EA3682 CRC64;
     MEHKDNSKMY GTTILCIRRN NHVIIAGDGQ VSLGHTVMKN SAKKVKRLAN DTVITGFAGA
     TADAFTLFER LEGKLEKHPG QLLRACVELA KDWRMDRYLR RLEAMMIVAD KSVSLVISGN
     GDVLEPENGI AAIGSGGNYA LAAAKALCES NDKFSQNMTL EYIVTTAMNI AAEICIYTNN
     NIIMEKIED