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ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Caseinolytic protease) (Endopeptidase Clp) (Stress protein G7)

 CLPP_BACSU              Reviewed;         197 AA.
P80244; O08433;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
28-FEB-2018, entry version 138.
RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
AltName: Full=Caseinolytic protease;
AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
AltName: Full=Stress protein G7;
Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=yvdN;
OrderedLocusNames=BSU34540;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY STRESS.
PubMed=9643546; DOI=10.1046/j.1365-2958.1998.00840.x;
Gerth U., Kruger E., Derre I., Msadek T., Hecker M.;
"Stress induction of the Bacillus subtilis clpP gene encoding a
homologue of the proteolytic component of the Clp protease and the
involvement of ClpP and ClpX in stress tolerance.";
Mol. Microbiol. 28:787-802(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Denizot F.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
PROTEIN SEQUENCE OF 1-24, AND INDUCTION BY STRESS.
STRAIN=168 / IS58;
PubMed=8012595; DOI=10.1099/00221287-140-4-741;
Voelker U., Engelmann S., Maul B., Riethdorf S., Voelker A.,
Schmid R., Mach H., Hecker M.;
"Analysis of the induction of general stress proteins of Bacillus
subtilis.";
Microbiology 140:741-752(1994).
[5]
PROTEIN SEQUENCE OF 1-21, AND INDUCTION BY STRESS.
STRAIN=168 / IS58;
PubMed=1362210; DOI=10.1099/00221287-138-10-2125;
Voelker U., Mach H., Schmid R., Hecker M.;
"Stress proteins and cross-protection by heat shock and salt stress in
Bacillus subtilis.";
J. Gen. Microbiol. 138:2125-2135(1992).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168 / Marburg / 1012;
PubMed=11395451; DOI=10.1128/JB.183.13.3885-3889.2001;
Wiegert T., Schumann W.;
"SsrA-mediated tagging in Bacillus subtilis.";
J. Bacteriol. 183:3885-3889(2001).
[7]
FUNCTION IN RSIW DEGRADATION.
PubMed=16899079; DOI=10.1111/j.1365-2958.2006.05323.x;
Zellmeier S., Schumann W., Wiegert T.;
"Involvement of Clp protease activity in modulating the Bacillus
subtilis sigma-W stress response.";
Mol. Microbiol. 61:1569-1582(2006).
-!- FUNCTION: Cleaves peptides in various proteins in a process that
requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
major role in the degradation of misfolded proteins (By
similarity). ClpXP is involved in the complete degradation of the
site-2 clipped anti-sigma-W factor RsiW. This results in the
release of SigW and the transcription activation of the genes
under the control of the sigma-W factor (PubMed:16899079).
Probably the major protease that degrades proteins tagged by
trans-translation (PubMed:11395451). {ECO:0000255|HAMAP-
Rule:MF_00444, ECO:0000269|PubMed:11395451,
ECO:0000269|PubMed:16899079}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
the presence of ATP and magnesium. Alpha-casein is the usual test
substrate. In the absence of ATP, only oligopeptides shorter than
five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-
Leu- and -Tyr-|-Trp bonds also occurs). {ECO:0000255|HAMAP-
Rule:MF_00444}.
-!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
which stack back to back to give a disk-like structure with a
central cavity, resembling the structure of eukaryotic proteasomes
(By similarity). Forms large heterooligomeric complexes consisting
of an ATPase component (ClpX, ClpC or ClpE) and a proteolytic
component (ClpP). {ECO:0000255|HAMAP-Rule:MF_00444}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-8165631, EBI-8165631;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
-!- INDUCTION: By heat shock, salt stress, ethanol stress, oxidative
stress, glucose limitation and oxygen limitation.
{ECO:0000269|PubMed:1362210, ECO:0000269|PubMed:8012595,
ECO:0000269|PubMed:9643546}.
-!- DISRUPTION PHENOTYPE: No degradation of trans-translationally
tagged-peptides. {ECO:0000269|PubMed:11395451}.
-!- SIMILARITY: Belongs to the peptidase S14 family.
{ECO:0000255|HAMAP-Rule:MF_00444}.
-----------------------------------------------------------------------
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EMBL; U59754; AAC46381.1; -; Genomic_DNA.
EMBL; Z94043; CAB08043.1; -; Genomic_DNA.
EMBL; AL009126; CAB15459.1; -; Genomic_DNA.
PIR; B69601; B69601.
RefSeq; NP_391334.1; NC_000964.3.
RefSeq; WP_003228214.1; NZ_JNCM01000033.1.
PDB; 3KTG; X-ray; 2.40 A; A/B/C/D/E/F/G=2-197.
PDB; 3KTH; X-ray; 3.00 A; A/B/C/D/E/F/G=2-197.
PDB; 3KTI; X-ray; 2.00 A; A/B/C/D/E/F/G=2-197.
PDB; 3KTJ; X-ray; 2.60 A; A/B/C/D/E/F/G=2-197.
PDB; 3KTK; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-197.
PDB; 3TT6; X-ray; 2.59 A; A/B/C/D/E/F/G=2-197.
PDB; 3TT7; X-ray; 2.56 A; A/B/C/D/E/F/G=1-197.
PDBsum; 3KTG; -.
PDBsum; 3KTH; -.
PDBsum; 3KTI; -.
PDBsum; 3KTJ; -.
PDBsum; 3KTK; -.
PDBsum; 3TT6; -.
PDBsum; 3TT7; -.
ProteinModelPortal; P80244; -.
SMR; P80244; -.
DIP; DIP-43711N; -.
IntAct; P80244; 1.
MINT; P80244; -.
STRING; 224308.Bsubs1_010100018711; -.
ChEMBL; CHEMBL2146309; -.
MEROPS; S14.001; -.
PaxDb; P80244; -.
PRIDE; P80244; -.
EnsemblBacteria; CAB15459; CAB15459; BSU34540.
GeneID; 938625; -.
KEGG; bsu:BSU34540; -.
PATRIC; fig|224308.179.peg.3741; -.
eggNOG; ENOG4105CCQ; Bacteria.
eggNOG; COG0740; LUCA.
HOGENOM; HOG000285833; -.
InParanoid; P80244; -.
KO; K01358; -.
OMA; YERWIDI; -.
PhylomeDB; P80244; -.
BioCyc; BSUB:BSU34540-MONOMER; -.
BRENDA; 3.4.21.92; 658.
EvolutionaryTrace; P80244; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004176; F:ATP-dependent peptidase activity; IMP:CACAO.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
CDD; cd07017; S14_ClpP_2; 1.
HAMAP; MF_00444; ClpP; 1.
InterPro; IPR001907; ClpP.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR023562; ClpP/TepA.
InterPro; IPR033135; ClpP_His_AS.
InterPro; IPR018215; ClpP_Ser_AS.
PANTHER; PTHR10381; PTHR10381; 1.
Pfam; PF00574; CLP_protease; 1.
PRINTS; PR00127; CLPPROTEASEP.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR00493; clpP; 1.
PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PROSITE; PS00381; CLP_PROTEASE_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Protease; Reference proteome; Serine protease;
Stress response.
CHAIN 1 197 ATP-dependent Clp protease proteolytic
subunit.
/FTId=PRO_0000179501.
ACT_SITE 98 98 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_00444}.
ACT_SITE 123 123 {ECO:0000255|HAMAP-Rule:MF_00444}.
HELIX 20 26 {ECO:0000244|PDB:3KTI}.
STRAND 29 32 {ECO:0000244|PDB:3KTI}.
HELIX 38 54 {ECO:0000244|PDB:3KTI}.
STRAND 56 58 {ECO:0000244|PDB:3KTI}.
STRAND 60 66 {ECO:0000244|PDB:3KTI}.
HELIX 71 83 {ECO:0000244|PDB:3KTI}.
STRAND 84 86 {ECO:0000244|PDB:3KTI}.
STRAND 88 97 {ECO:0000244|PDB:3KTI}.
HELIX 99 105 {ECO:0000244|PDB:3KTI}.
STRAND 112 114 {ECO:0000244|PDB:3KTI}.
STRAND 119 122 {ECO:0000244|PDB:3KTI}.
STRAND 126 132 {ECO:0000244|PDB:3KTK}.
HELIX 133 158 {ECO:0000244|PDB:3KTI}.
HELIX 162 168 {ECO:0000244|PDB:3KTI}.
STRAND 173 176 {ECO:0000244|PDB:3KTI}.
HELIX 177 183 {ECO:0000244|PDB:3KTI}.
STRAND 187 189 {ECO:0000244|PDB:3KTI}.
SEQUENCE 197 AA; 21682 MW; 5D4D4BD548DC45A0 CRC64;
MNLIPTVIEQ TNRGERAYDI YSRLLKDRII MLGSAIDDNV ANSIVSQLLF LAAEDPEKEI
SLYINSPGGS ITAGMAIYDT MQFIKPKVST ICIGMAASMG AFLLAAGEKG KRYALPNSEV
MIHQPLGGAQ GQATEIEIAA KRILLLRDKL NKVLAERTGQ PLEVIERDTD RDNFKSAEEA
LEYGLIDKIL THTEDKK


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