CLPP_FRATT
ID CLPP_FRATT Reviewed; 201 AA.
AC Q5NH47;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=FTT_0624;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45257.1; -; Genomic_DNA.
DR RefSeq; WP_003015534.1; NZ_CP010290.1.
DR RefSeq; YP_169645.1; NC_006570.2.
DR PDB; 3P2L; X-ray; 2.30 A; A/B/C/D/E/F/G=4-201.
DR PDB; 5G1Q; X-ray; 2.84 A; A/B/C/D/E/F/G=1-201.
DR PDB; 5G1R; X-ray; 1.90 A; A/B/C/D/E/F/G=1-201.
DR PDB; 5G1S; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=1-201.
DR PDBsum; 3P2L; -.
DR PDBsum; 5G1Q; -.
DR PDBsum; 5G1R; -.
DR PDBsum; 5G1S; -.
DR AlphaFoldDB; Q5NH47; -.
DR SMR; Q5NH47; -.
DR IntAct; Q5NH47; 1.
DR STRING; 177416.FTT_0624; -.
DR MEROPS; S14.001; -.
DR DNASU; 3192361; -.
DR EnsemblBacteria; CAG45257; CAG45257; FTT_0624.
DR KEGG; ftu:FTT_0624; -.
DR eggNOG; COG0740; Bacteria.
DR OMA; RDYWMKA; -.
DR EvolutionaryTrace; Q5NH47; -.
DR Proteomes; UP000001174; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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..201
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179558"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 126
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5G1R"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5G1S"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:5G1S"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5G1S"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5G1S"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5G1S"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:3P2L"
FT HELIX 136..161
FT /evidence="ECO:0007829|PDB:5G1S"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:5G1S"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5G1Q"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5G1S"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:5G1S"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5G1S"
SQ SEQUENCE 201 AA; 22150 MW; CE00A6E52FC18FD6 CRC64;
MITNNLVPTV IEKTAGGERA FDIYSRLLKE RIVFLNGEVN DHSANLVIAQ LLFLESEDPD
KDIYFYINSP GGMVTAGMGV YDTMQFIKPD VSTICIGLAA SMGSLLLAGG AKGKRYSLPS
SQIMIHQPLG GFRGQASDIE IHAKNILRIK DRLNKVLAHH TGQDLETIVK DTDRDNFMMA
DEAKAYGLID HVIESREAII K
