HSLV_MANHA
ID HSLV_MANHA Reviewed; 173 AA.
AC P49617;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
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};
DE AltName: Full=Protein LapC;
GN Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248}; Synonyms=lapC;
OS Mannheimia haemolytica (Pasteurella haemolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=75985;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A1 / PH101;
RX PubMed=8359916; DOI=10.1128/iai.61.9.3942-3951.1993;
RA Highlander S.K., Wickersham E.A., Garza O., Weinstock G.M.;
RT "Expression of the Pasteurella haemolytica leukotoxin is inhibited by a
RT locus that encodes an ATP-binding cassette homolog.";
RL Infect. Immun. 61:3942-3951(1993).
RN [2]
RP ERRATUM OF PUBMED:8359916.
RA Highlander S.K., Wickersham E.A., Garza O., Weinstock G.M.;
RL Infect. Immun. 61:5431-5431(1993).
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; M59210; AAA25533.1; -; Genomic_DNA.
DR RefSeq; WP_006248017.1; NZ_VAJK01000035.1.
DR AlphaFoldDB; P49617; -.
DR SMR; P49617; -.
DR STRING; 75985.WC39_13345; -.
DR MEROPS; T01.006; -.
DR GeneID; 67370323; -.
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 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..173
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_0000148128"
FT ACT_SITE 2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 158
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 161
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 164
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
SQ SEQUENCE 173 AA; 18817 MW; E13D773F587DE711 CRC64;
MTTIVCVRKD GKVAIGGDGQ ATLGNCIEKG TVRKVRRLYK DKVVTGFAGS TADAFILRDL
FEKKLELHQG HLVKSAVELA KEWRTERALR RLEAMMIVAN DSEFLLVSGS GDVIEPEQDV
LAIGSGGNYA KAAALALLRT ENNLSAKEIV AEALKIAGDI DIYSNYNHVI EEV