HSLV_HAEIN
ID HSLV_HAEIN Reviewed; 175 AA.
AC P43772;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=HI_0496;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15037245; DOI=10.1016/j.jsb.2003.11.003;
RA Kwon A.-R., Trame C.B., McKay D.B.;
RT "Kinetics of protein substrate degradation by HslUV.";
RL J. Struct. Biol. 146:141-147(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLU.
RX PubMed=11106733; DOI=10.1016/s0092-8674(00)00166-5;
RA Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., McKay D.B.;
RT "Crystal and solution structures of an HslUV protease-chaperone complex.";
RL Cell 103:633-643(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH POTASSIUM OR SODIUM.
RX PubMed=11717526; DOI=10.1107/s090744490101575x;
RA Sousa M.C., McKay D.B.;
RT "Structure of Haemophilus influenzae HslV protein at 1.9 A resolution,
RT revealing a cation-binding site near the catalytic site.";
RL Acta Crystallogr. D 57:1950-1954(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLU AND
RP INHIBITOR, AND ACTIVITY REGULATION.
RX PubMed=12054822; DOI=10.1016/s0022-2836(02)00145-6;
RA Sousa M.C., Kessler B.M., Overkleeft H.S., McKay D.B.;
RT "Crystal structure of HslUV complexed with a vinyl sulfone inhibitor:
RT corroboration of a proposed mechanism of allosteric activation of HslV by
RT HslU.";
RL J. Mol. Biol. 318:779-785(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLU;
RP MAGNESIUM; ADP AND INHIBITOR.
RX PubMed=12823960; DOI=10.1016/s0022-2836(03)00580-1;
RA Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B.;
RT "Structure and reactivity of an asymmetric complex between HslV and I-
RT domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome.";
RL J. Mol. Biol. 330:185-195(2003).
CC -!- FUNCTION: Protease subunit of a proteasome-like degradation complex
CC believed to be a general protein degrading machinery.
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, ECO:0000269|PubMed:12054822}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for Arc-H(6)-SulA(CT) {ECO:0000269|PubMed:15037245};
CC Note=Arc-H(6)-SulA(CT) is a construct consisting of the Arc repressor
CC protein fused to 6 His residues and the 11 carboxy terminal residues
CC of SulA.;
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, ECO:0000269|PubMed:11106733,
CC ECO:0000269|PubMed:11717526, ECO:0000269|PubMed:12054822,
CC ECO:0000269|PubMed:12823960}.
CC -!- INTERACTION:
CC P43772; P43773: hslU; NbExp=4; IntAct=EBI-1030290, EBI-1030296;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC22153.1; -; Genomic_DNA.
DR PIR; C64072; C64072.
DR RefSeq; NP_438654.1; NC_000907.1.
DR RefSeq; WP_005649427.1; NC_000907.1.
DR PDB; 1G3I; X-ray; 3.41 A; G/H/I/J/K/L/M/N/O/P/Q/R=2-175.
DR PDB; 1G3K; X-ray; 1.90 A; A/B/C=2-175.
DR PDB; 1JJW; X-ray; 1.90 A; A/B/C=2-175.
DR PDB; 1KYI; X-ray; 3.10 A; G/H/I/J/K/L/M/N/O/P/Q/R=2-175.
DR PDB; 1OFH; X-ray; 2.50 A; G/H/I/L/M/N=2-175.
DR PDB; 1OFI; X-ray; 3.20 A; G/H/I/L/M/N=2-175.
DR PDBsum; 1G3I; -.
DR PDBsum; 1G3K; -.
DR PDBsum; 1JJW; -.
DR PDBsum; 1KYI; -.
DR PDBsum; 1OFH; -.
DR PDBsum; 1OFI; -.
DR AlphaFoldDB; P43772; -.
DR SMR; P43772; -.
DR DIP; DIP-6176N; -.
DR IntAct; P43772; 1.
DR STRING; 71421.HI_0496; -.
DR MEROPS; T01.006; -.
DR EnsemblBacteria; AAC22153; AAC22153; HI_0496.
DR KEGG; hin:HI_0496; -.
DR PATRIC; fig|71421.8.peg.514; -.
DR eggNOG; COG5405; Bacteria.
DR HOGENOM; CLU_093872_1_0_6; -.
DR OMA; IMKGNAR; -.
DR PhylomeDB; P43772; -.
DR BioCyc; HINF71421:G1GJ1-509-MON; -.
DR BRENDA; 3.4.25.2; 2529.
DR EvolutionaryTrace; P43772; -.
DR Proteomes; UP000000579; 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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Sodium; Threonine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..175
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_0000148111"
FT ACT_SITE 2
FT BINDING 158
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 161
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 164
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1G3K"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1G3K"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:1G3K"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1G3K"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1G3K"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1G3K"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1G3K"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:1G3K"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:1G3K"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1G3K"
SQ SEQUENCE 175 AA; 19012 MW; CEA1C77B7AB2724C CRC64;
MTTIVSVRRN GQVVVGGDGQ VSLGNTVMKG NARKVRRLYN GKVLAGFAGG TADAFTLFEL
FERKLEMHQG HLLKSAVELA KDWRTDRALR KLEAMLIVAD EKESLIITGI GDVVQPEEDQ
ILAIGSGGNY ALSAARALVE NTELSAHEIV EKSLRIAGDI CVFTNTNFTI EELPN
