CLPP_STRR6
ID CLPP_STRR6 Reviewed; 196 AA.
AC P63788; P58279;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=spr0656;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
CC -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC major role in the degradation of misfolded proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC stack back to back to give a disk-like structure with a central cavity,
CC resembling the structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
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DR EMBL; AE007317; AAK99460.1; -; Genomic_DNA.
DR PIR; H97953; H97953.
DR RefSeq; NP_358250.1; NC_003098.1.
DR RefSeq; WP_000613477.1; NC_003098.1.
DR PDB; 1Y7O; X-ray; 2.51 A; A/B/C/D/E/F/G=1-196.
DR PDBsum; 1Y7O; -.
DR AlphaFoldDB; P63788; -.
DR SMR; P63788; -.
DR STRING; 171101.spr0656; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; AAK99460; AAK99460; spr0656.
DR GeneID; 60234145; -.
DR GeneID; 66805894; -.
DR KEGG; spr:spr0656; -.
DR PATRIC; fig|171101.6.peg.728; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_9; -.
DR OMA; RDYWMKA; -.
DR EvolutionaryTrace; P63788; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..196
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179671"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 121
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1Y7O"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1Y7O"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:1Y7O"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1Y7O"
FT HELIX 140..158
FT /evidence="ECO:0007829|PDB:1Y7O"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1Y7O"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:1Y7O"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1Y7O"
SQ SEQUENCE 196 AA; 21358 MW; 2C6C3A820A290B2B CRC64;
MIPVVIEQTS RGERSYDIYS RLLKDRIIML TGPVEDNMAN SVIAQLLFLD AQDSTKDIYL
YVNTPGGSVS AGLAIVDTMN FIKADVQTIV MGMAASMGTV IASSGAKGKR FMLPNAEYMI
HQPMGGTGGG TQQTDMAIAA EHLLKTRNTL EKILAENSGQ SMEKVHADAE RDNWMSAQET
LEYGFIDEIM ANNSLN
