ID HSLV_ECOLI Reviewed; 176 AA. AC P0A7B8; P31059; P97542; Q2M8M8; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 05-SEP-2012, entry version 76. DE RecName: Full=ATP-dependent protease subunit HslV; DE EC=3.4.25.2; DE AltName: Full=Heat shock protein HslV; GN Name=hslV; Synonyms=htpO, yiiC; OrderedLocusNames=b3932, JW3903; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94063501; PubMed=8244018; DOI=10.1016/0378-1119(93)90167-2; RA Chuang S.E., Burland V., Plunkett G. III, Daniels D.L., Blattner F.R.; RT "Sequence analysis of four new heat-shock genes constituting the RT hslTS/ibpAB and hslVU operons in Escherichia coli."; RL Gene 134:1-6(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=93347969; PubMed=8346018; DOI=10.1093/nar/21.15.3391; RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome. III. DNA sequence of the RT region from 87.2 to 89.2 minutes."; RL Nucleic Acids Res. 21:3391-3398(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. RX MEDLINE=97166005; PubMed=9013898; DOI=10.1016/S0014-5793(96)01485-8; RA Ohya S., Takii T., Yamazaki H., Matsumori M., Onozaki K., Watanabe M., RA Imaizumi Y.; RT "Molecular cloning of a novel gene involved in serotonin receptor- RT mediated signal transduction in rat stomach."; RL FEBS Lett. 401:252-258(1997). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88. RA Dai K., Xu Y., Lutkenhaus J.; RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND SUBSTRATE SPECIFICITY. RX PubMed=8662828; DOI=10.1074/jbc.271.24.14035; RA Yoo S.J., Seol J.H., Shin D.H., Rohrwild M., Kang M.-S., Tanaka K., RA Goldberg A.L., Chung C.H.; RT "Purification and characterization of the heat shock proteins HslV and RT HslU that form a new ATP-dependent protease in Escherichia coli."; RL J. Biol. Chem. 271:14035-14040(1996). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND PROTEIN SEQUENCE OF N-TERMINUS. RX PubMed=8650174; DOI=10.1073/pnas.93.12.5808; RA Rohrwild M., Coux O., Huang H.-C., Moerschell R.P., Yoo S.J., RA Seol J.H., Chung C.H., Goldberg A.L.; RT "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli RT related to the eukaryotic proteasome."; RL Proc. Natl. Acad. Sci. U.S.A. 93:5808-5813(1996). RN [9] RP EFFECTS OF ATP BINDING ON COMPLEX FORMATION. RX PubMed=9299555; DOI=10.1006/bbrc.1997.7341; RA Yoo S.J., Seol J.H., Seong I.S., Kang M.-S., Chung C.H.; RT "ATP binding, but not its hydrolysis, is required for assembly and RT proteolytic activity of the HslVU protease in Escherichia coli."; RL Biochem. Biophys. Res. Commun. 238:581-585(1997). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=9288941; DOI=10.1111/j.1432-1033.1997.01143.x; RA Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.-S., Goldberg A.L., RA Chung C.H.; RT "The heat-shock protein HslVU from Escherichia coli is a protein- RT activated ATPase as well as an ATP-dependent proteinase."; RL Eur. J. Biochem. 247:1143-1150(1997). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9393683; RA Kanemori M., Nishihara K., Yanagi H., Yura T.; RT "Synergistic roles of HslVU and other ATP-dependent proteases in RT controlling in vivo turnover of sigma32 and abnormal proteins in RT Escherichia coli."; RL J. Bacteriol. 179:7219-7225(1997). RN [12] RP MUTAGENESIS OF THR-2; THR-3; SER-6; SER-104; SER-125; SER-144 AND RP SER-173, AND ACTIVE SITE. RX MEDLINE=97400195; PubMed=9257689; DOI=10.1016/S0014-5793(97)00742-4; RA Yoo S.J., Shim Y.K., Seong I.S., Seol J.H., Kang M.-S., Chung C.H.; RT "Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the RT proteolytic component of the ATP-dependent HslVU protease."; RL FEBS Lett. 412:57-60(1997). RN [13] RP MUTAGENESIS OF CYS-160. RX MEDLINE=98389714; PubMed=9722513; DOI=10.1074/jbc.273.36.22929; RA Yoo S.J., Kim H.H., Shin D.H., Lee C.S., Seong I.S., Seol J.H., RA Shimbara N., Tanaka K., Chung C.H.; RT "Effects of the cys mutations on structure and function of the ATP- RT dependent HslVU protease in Escherichia coli. The Cys287 to Val RT mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from RT ATP hydrolysis."; RL J. Biol. Chem. 273:22929-22935(1998). RN [14] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10452560; DOI=10.1016/S0014-5793(99)00935-7; RA Seong I.S., Oh J.Y., Yoo S.J., Seol J.H., Chung C.H.; RT "ATP-dependent degradation of SulA, a cell division inhibitor, by the RT HslVU protease in Escherichia coli."; RL FEBS Lett. 456:211-214(1999). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION. RX PubMed=10419524; DOI=10.1074/jbc.274.31.22002; RA Kanemori M., Yanagi H., Yura T.; RT "Marked instability of the sigma(32) heat shock transcription factor RT at high temperature. Implications for heat shock regulation."; RL J. Biol. Chem. 274:22002-22007(1999). RN [16] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15696175; DOI=10.1038/nsmb898; RA Burton R.E., Baker T.A., Sauer R.T.; RT "Nucleotide-dependent substrate recognition by the AAA+ HslUV RT protease."; RL Nat. Struct. Mol. Biol. 12:245-251(2005). RN [17] RP REACTION MECHANISM. RX PubMed=19801685; DOI=10.1074/jbc.M109.045807; RA Lee J.W., Park E., Jeong M.S., Jeon Y.J., Eom S.H., Seol J.H., RA Chung C.H.; RT "HslVU ATP-dependent protease utilizes maximally six among twelve RT threonine active sites during proteolysis."; RL J. Biol. Chem. 284:33475-33484(2009). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS), AND SUBUNIT. RX MEDLINE=97322325; PubMed=9177170; DOI=10.1073/pnas.94.12.6070; RA Bochtler M., Ditzel L., Groll M., Huber R.; RT "Crystal structure of heat shock locus V (HslV) from Escherichia RT coli."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6070-6074(1997). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH HSLU AND ATP RP ANALOG. RX MEDLINE=20155479; PubMed=10693812; DOI=10.1038/35001629; RA Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., RA Huber R.; RT "The structures of HslU and the ATP-dependent protease HslU-HslV."; RL Nature 403:800-805(2000). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176. RX PubMed=11114186; DOI=10.1073/pnas.250491797; RA Song H.K., Hartmann C., Ramachandran R., Bochtler M., Behrendt R., RA Moroder L., Huber R.; RT "Mutational studies on HslU and its docking mode with HslV."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14103-14108(2000). RN [21] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-175. RX PubMed=11250202; DOI=10.1016/S0969-2126(01)00570-6; RA Wang J., Song J.J., Franklin M.C., Kamtekar S., Im Y.J., Rho S.H., RA Seong I.S., Lee C.S., Chung C.H., Eom S.H.; RT "Crystal structures of the HslVU peptidase-ATPase complex reveal an RT ATP-dependent proteolysis mechanism."; RL Structure 9:177-184(2001). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176. RX PubMed=11709174; DOI=10.1016/S0969-2126(01)00670-0; RA Wang J., Song J.J., Seong I.S., Franklin M.C., Kamtekar S., Eom S.H., RA Chung C.H.; RT "Nucleotide-dependent conformational changes in a protease-associated RT ATPase HslU."; RL Structure 9:1107-1116(2001). CC -!- FUNCTION: Protease subunit of a proteasome-like degradation CC complex believed to be a general protein degrading machinery. The CC complex has been shown to be involved in the specific degradation CC of heat shock induced transcription factors such as RpoH and SulA. CC In addition, small hydrophobic peptides are also hydrolyzed by CC HslV. HslV has weak protease activity even in the absence of HslU, CC but this activity is induced more than 100-fold in the presence of CC HslU. HslU recognizes protein substrates and unfolds these before CC guiding them to HslV for hydrolysis. HslV is not believed to CC degrade folded proteins. CC -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. CC -!- ENZYME REGULATION: Allosterically activated by HslU binding CC (Probable). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5.2 uM for Arc-MYL-st11 (at 37 degrees Celsius); CC Note=Arc is a repressor protein, Arc-MYL-st11 is a hyperstable CC variant of Arc; CC Temperature dependence: CC Optimum temperature is 55 degrees Celsius; CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on CC each side by a ring-shaped HslU homohexamer. The assembly of the CC HslU/HslV complex is dependent on binding of ATP. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-552265, EBI-552265; CC P0A6H5:hslU; NbExp=7; IntAct=EBI-552265, EBI-369317; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By heat shock. CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. CC -!- CAUTION: PubMed:9013898 sequence is supposed to originate from rat CC but, based on sequence similarity, it seems that this is a case of CC bacterial contamination from E.coli. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L19201; AAB03064.1; -; Genomic_DNA. DR EMBL; U00096; AAC76914.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77378.1; -; Genomic_DNA. DR EMBL; D89965; BAA14040.1; ALT_SEQ; mRNA. DR EMBL; L14281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; JT0760; JT0760. DR RefSeq; NP_418367.1; NC_000913.2. DR RefSeq; YP_491519.1; NC_007779.1. DR PDB; 1E94; X-ray; 2.80 A; A/B/C/D=2-176. DR PDB; 1G4A; X-ray; 3.00 A; A/B/C/D=2-175. DR PDB; 1G4B; X-ray; 7.00 A; M/N/O/P=2-175. DR PDB; 1HQY; X-ray; 2.80 A; A/B/C/D=2-176. DR PDB; 1HT1; X-ray; 2.80 A; A/B/C/D/V/X/Y/Z=2-176. DR PDB; 1HT2; X-ray; 2.80 A; A/B/C/D/I/J/K/L=2-176. DR PDB; 1NED; X-ray; 3.80 A; A/B/C=2-176. DR PDBsum; 1E94; -. DR PDBsum; 1G4A; -. DR PDBsum; 1G4B; -. DR PDBsum; 1HQY; -. DR PDBsum; 1HT1; -. DR PDBsum; 1HT2; -. DR PDBsum; 1NED; -. DR ProteinModelPortal; P0A7B8; -. DR SMR; P0A7B8; 2-175. DR DIP; DIP-35866N; -. DR IntAct; P0A7B8; 32. DR MINT; MINT-1218940; -. DR MEROPS; T01.006; -. DR ECO2DBASE; G021.0; 6TH EDITION. DR SWISS-2DPAGE; P0A7B8; -. DR PRIDE; P0A7B8; -. DR EnsemblBacteria; EBESCT00000003716; EBESCP00000003716; EBESCG00000003037. DR EnsemblBacteria; EBESCT00000017074; EBESCP00000016365; EBESCG00000016133. DR GeneID; 12932787; -. DR GeneID; 948429; -. DR GenomeReviews; AP009048_GR; JW3903. DR GenomeReviews; U00096_GR; b3932. DR KEGG; eco:b3932; -. DR PATRIC; 32123379; VBIEscCol129921_4050. DR EchoBASE; EB1627; -. DR EcoGene; EG11676; hslV. DR eggNOG; COG5405; -. DR HOGENOM; HOG000064533; -. DR KO; K01419; -. DR OMA; WRTDKYL; -. DR ProtClustDB; PRK05456; -. DR BioCyc; EcoCyc:EG11676-MONOMER; -. DR EvolutionaryTrace; P0A7B8; -. DR Genevestigator; P0A7B8; -. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro. 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 cellular protein catabolic process; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki. DR HAMAP; MF_00248; HslV; 1; -. DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su. DR InterPro; IPR001353; Proteasome_sua/b. DR PANTHER; PTHR11599:SF38; PTHR11599:SF38; 1. DR Pfam; PF00227; Proteasome; 1. DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm; KW Direct protein sequencing; Hydrolase; Metal-binding; Protease; KW Reference proteome; Sodium; Stress response; Threonine protease. FT INIT_MET 1 1 Removed. FT CHAIN 2 176 ATP-dependent protease subunit HslV. FT /FTId=PRO_0000148105. FT ACT_SITE 2 2 FT METAL 157 157 Sodium; via carbonyl oxygen. FT METAL 160 160 Sodium; via carbonyl oxygen. FT METAL 163 163 Sodium; via carbonyl oxygen. FT MUTAGEN 2 2 T->S: 80% reduced protease activity in FT the absence of HslU. Almost no effect in FT the presence of HslU. FT MUTAGEN 2 2 T->V: No protease activity. FT MUTAGEN 3 3 T->S,V: 80% reduced protease activity. FT MUTAGEN 6 6 S->A: No effect. FT MUTAGEN 104 104 S->A: 50% reduced protease activity. FT MUTAGEN 125 125 S->A: Almost no protease activity. FT MUTAGEN 144 144 S->A: No effect. FT MUTAGEN 160 160 C->A,S: No protease activity. Cannot form FT complexes with HslU. FT MUTAGEN 173 173 S->A: Almost no protease activity. FT STRAND 3 8 FT STRAND 10 17 FT STRAND 21 23 FT STRAND 26 30 FT STRAND 35 38 FT TURN 39 42 FT STRAND 43 49 FT HELIX 51 66 FT TURN 67 70 FT HELIX 72 85 FT HELIX 89 91 FT STRAND 94 99 FT STRAND 104 108 FT TURN 109 111 FT STRAND 112 114 FT TURN 117 119 FT STRAND 121 124 FT HELIX 127 138 FT HELIX 145 159 FT STRAND 168 173 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 //