CLPQ_BACSU
ID CLPQ_BACSU Reviewed; 181 AA.
AC P39070;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-dependent protease subunit ClpQ;
DE EC=3.4.21.-;
GN Name=clpQ; Synonyms=codW, hslV; OrderedLocusNames=BSU16150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=7783641; DOI=10.1111/j.1365-2958.1995.tb02378.x;
RA Slack F.J., Serror P., Joyce E., Sonenshein A.L.;
RT "A gene required for nutritional repression of the Bacillus subtilis
RT dipeptide permease operon.";
RL Mol. Microbiol. 15:689-702(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PY143;
RA Walther T., Hofemeister J.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP PROTEIN SEQUENCE OF 2-8, CATALYTIC ACTIVITY, FUNCTION AS A SERINE PROTEASE,
RP MUTAGENESIS OF SER-2; ALA-6; THR-7 AND THR-8, AND MASS SPECTROMETRY.
RX PubMed=11179218; DOI=10.1093/emboj/20.4.734;
RA Kang M.S., Lim B.K., Seong I.S., Seol J.H., Tanahashi N., Tanaka K.,
RA Chung C.H.;
RT "The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-
RT terminal serine protease.";
RL EMBO J. 20:734-742(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (4.16 ANGSTROMS) IN COMPLEX WITH E.COLI HSLU AND ADP.
RX PubMed=15983416; DOI=10.1107/s0907444905009546;
RA Wang J., Rho S.H., Park H.H., Eom S.H.;
RT "Correction of X-ray intensities from an HslV-HslU co-crystal containing
RT lattice-translocation defects.";
RL Acta Crystallogr. D 61:932-941(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-181 IN COMPLEX WITH SODIUM IONS.
RX PubMed=17979190; DOI=10.1002/prot.21758;
RA Rho S.H., Park H.H., Kang G.B., Im Y.J., Kang M.S., Lim B.K., Seong I.S.,
RA Seol J., Chung C.H., Wang J., Eom S.H.;
RT "Crystal structure of Bacillus subtilis CodW, a noncanonical HslV-like
RT peptidase with an impaired catalytic apparatus.";
RL Proteins 71:1020-1026(2008).
CC -!- FUNCTION: Protease subunit of a proteasome-like degradation complex.
CC {ECO:0000269|PubMed:11179218}.
CC -!- SUBUNIT: A double ring-shaped homohexamer of ClpQ is capped on each
CC side by a ring-shaped ClpY homohexamer. The assembly of the ClpQ/ClpY
CC complex is dependent on binding of ATP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=19345.7; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:11179218};
CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC {ECO:0000305}.
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DR EMBL; U13634; AAB03370.1; -; Genomic_DNA.
DR EMBL; Z33639; CAA83919.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13488.1; -; Genomic_DNA.
DR PIR; S61494; S61494.
DR RefSeq; NP_389497.1; NC_000964.3.
DR RefSeq; WP_003238555.1; NZ_JNCM01000035.1.
DR PDB; 1YYF; X-ray; 4.16 A; C/D=1-181.
DR PDB; 2Z3A; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-181.
DR PDB; 2Z3B; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-181.
DR PDBsum; 1YYF; -.
DR PDBsum; 2Z3A; -.
DR PDBsum; 2Z3B; -.
DR AlphaFoldDB; P39070; -.
DR SMR; P39070; -.
DR STRING; 224308.BSU16150; -.
DR MEROPS; T01.007; -.
DR PaxDb; P39070; -.
DR PRIDE; P39070; -.
DR EnsemblBacteria; CAB13488; CAB13488; BSU_16150.
DR GeneID; 938111; -.
DR KEGG; bsu:BSU16150; -.
DR PATRIC; fig|224308.179.peg.1755; -.
DR eggNOG; COG5405; Bacteria.
DR InParanoid; P39070; -.
DR OMA; IMKGNAR; -.
DR PhylomeDB; P39070; -.
DR BioCyc; BSUB:BSU16150-MON; -.
DR EvolutionaryTrace; P39070; -.
DR PRO; PR:P39070; -.
DR Proteomes; UP000001570; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
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; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Serine protease; Sodium.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11179218"
FT CHAIN 2..181
FT /note="ATP-dependent protease subunit ClpQ"
FT /id="PRO_0000026678"
FT ACT_SITE 2
FT BINDING 165
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 168
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 171
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT MUTAGEN 2
FT /note="S->A,T: Complete loss of protease activity."
FT /evidence="ECO:0000269|PubMed:11179218"
FT MUTAGEN 6
FT /note="A->G: No effect."
FT /evidence="ECO:0000269|PubMed:11179218"
FT MUTAGEN 7
FT /note="T->A: Complete loss of protease activity. The mutant
FT is only found as a monomer; when associated with A-8."
FT /evidence="ECO:0000269|PubMed:11179218"
FT MUTAGEN 8
FT /note="T->A: Complete loss of protease activity. The mutant
FT is only found as a monomer; when associated with A-7."
FT /evidence="ECO:0000269|PubMed:11179218"
FT CONFLICT 2..5
FT /note="Missing (in Ref. 2; CAA83919)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> R (in Ref. 2; CAA83919)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="E -> K (in Ref. 2; CAA83919)"
FT /evidence="ECO:0000305"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2Z3B"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2Z3B"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2Z3B"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:2Z3B"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2Z3B"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:2Z3B"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2Z3B"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:2Z3B"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2Z3B"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:2Z3B"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2Z3B"
SQ SEQUENCE 181 AA; 19478 MW; 95DC72474A41A97D CRC64;
MSSFHATTIF AVQHKGRSAM SGDGQVTFGQ AVVMKHTARK VRKLFNGKVL AGFAGSVADA
FTLFEKFEAK LEEYNGNLKR AAVELAKEWR SDKVLRKLEA MLIVMNQDTL LLVSGTGEVI
EPDDGILAIG SGGNYALAAG RALKKHAGES MSASEIARAA LETAGEICVY TNDQIILEEL
E
