CLPP_HELPY
ID CLPP_HELPY Reviewed; 196 AA.
AC P56156;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=HP_0794;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07842.1; -; Genomic_DNA.
DR PIR; B64619; B64619.
DR RefSeq; NP_207587.1; NC_000915.1.
DR RefSeq; WP_001853304.1; NC_018939.1.
DR PDB; 2ZL0; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-196.
DR PDB; 2ZL2; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-196.
DR PDB; 2ZL3; X-ray; 2.81 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-196.
DR PDB; 2ZL4; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-196.
DR PDBsum; 2ZL0; -.
DR PDBsum; 2ZL2; -.
DR PDBsum; 2ZL3; -.
DR PDBsum; 2ZL4; -.
DR AlphaFoldDB; P56156; -.
DR SMR; P56156; -.
DR DIP; DIP-3357N; -.
DR IntAct; P56156; 1.
DR MINT; P56156; -.
DR STRING; 85962.C694_04070; -.
DR MEROPS; S14.001; -.
DR PaxDb; P56156; -.
DR EnsemblBacteria; AAD07842; AAD07842; HP_0794.
DR KEGG; hpy:HP_0794; -.
DR PATRIC; fig|85962.8.peg.826; -.
DR eggNOG; COG0740; Bacteria.
DR OMA; RDYWMKA; -.
DR PhylomeDB; P56156; -.
DR EvolutionaryTrace; P56156; -.
DR Proteomes; UP000000429; 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 TIGRFAMs; TIGR00493; clpP; 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_0000179568"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 124
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:2ZL2"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2ZL2"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2ZL2"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:2ZL2"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2ZL2"
FT HELIX 134..159
FT /evidence="ECO:0007829|PDB:2ZL2"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2ZL2"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:2ZL2"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2ZL2"
SQ SEQUENCE 196 AA; 21526 MW; 4E19BE5FE44656B0 CRC64;
MMGYIPYVIE NTDRGERSYD IYSRLLKDRI VLLSGEINDS VASSIVAQLL FLEAEDPEKD
IGLYINSPGG VITSGLSIYD TMNFIRPDVS TICIGQAASM GAFLLSCGAK GKRFSLPHSR
IMIHQPLGGA QGQASDIEII SNEILRLKGL MNSILAQNSG QSLEQIAKDT DRDFYMSAKE
AKEYGLIDKV LQKNVK
