ID   HSLV_BORA1              Reviewed;         179 AA.
AC   Q2L1C6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=BAV0143;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(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; AM167904; CAJ47749.1; -; Genomic_DNA.
DR   RefSeq; WP_012415847.1; NC_010645.1.
DR   AlphaFoldDB; Q2L1C6; -.
DR   SMR; Q2L1C6; -.
DR   STRING; 360910.BAV0143; -.
DR   MEROPS; T01.006; -.
DR   EnsemblBacteria; CAJ47749; CAJ47749; BAV0143.
DR   GeneID; 41392071; -.
DR   KEGG; bav:BAV0143; -.
DR   eggNOG; COG5405; Bacteria.
DR   HOGENOM; CLU_093872_1_0_4; -.
DR   OMA; IMKGNAR; -.
DR   OrthoDB; 1129370at2; -.
DR   Proteomes; UP000001977; 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;
KW   Reference proteome; Sodium; Stress response; Threonine protease.
FT   CHAIN           1..179
FT                   /note="ATP-dependent protease subunit HslV"
FT                   /id="PRO_1000012581"
FT   ACT_SITE        7
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         162
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         165
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         168
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
SQ   SEQUENCE   179 AA;  19447 MW;  3669B968770AEB44 CRC64;
     MEQFHATTIV CVRRGNRVAL GGDGQVTLGN IVIKGTARKI RRLYHDKVLA GFAGATADAF
     TLQERFEAKL EKHQGHLMRA AVELTRDWRT DRVLRRLEAM LIVADAEHTL VLTGNGDVLE
     PEHGLAAIGS GGAYAQSAAL ALLRNTELPP ETIVKQSLEI AGDLCIYTNQ NHVIETLGG