HSLV_ECO55
ID HSLV_ECO55 Reviewed; 176 AA.
AC B7LA29;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Heat shock protein HslV {ECO:0000255|HAMAP-Rule:MF_00248};
GN Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248};
GN OrderedLocusNames=EC55989_4410;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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 -!- INDUCTION: By heat shock. {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; CU928145; CAV01137.1; -; Genomic_DNA.
DR RefSeq; WP_000208242.1; NC_011748.1.
DR PDB; 5JI2; X-ray; 3.31 A; A/B/C/D=1-176.
DR PDBsum; 5JI2; -.
DR AlphaFoldDB; B7LA29; -.
DR SMR; B7LA29; -.
DR MEROPS; T01.006; -.
DR EnsemblBacteria; CAV01137; CAV01137; EC55989_4410.
DR GeneID; 67417555; -.
DR KEGG; eck:EC55989_4410; -.
DR HOGENOM; CLU_093872_1_0_6; -.
DR OMA; IMKGNAR; -.
DR Proteomes; UP000000746; 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; Sodium; Stress response; Threonine protease.
FT CHAIN 1..176
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_1000125407"
FT ACT_SITE 2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 157
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 160
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT BINDING 163
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5JI2"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:5JI2"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:5JI2"
SQ SEQUENCE 176 AA; 19093 MW; 3B35E01F51486965 CRC64;
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG TADAFTLFEL
FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD ETASLIITGN GDVVQPENDL
IAIGSGGPYA QAAARALLEN TELSAREIAE KALDIAGDIC IYTNHFHTIE ELSYKA
