CLPP2_CHLTR
ID CLPP2_CHLTR Reviewed; 203 AA.
AC O84712;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 2 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 2 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP2 {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=CT_706;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC68301.1; -; Genomic_DNA.
DR PIR; C71481; C71481.
DR RefSeq; NP_220225.1; NC_000117.1.
DR RefSeq; WP_009872081.1; NC_000117.1.
DR PDB; 6X60; X-ray; 2.81 A; A/B/C/D/E/F/G=1-203.
DR PDBsum; 6X60; -.
DR AlphaFoldDB; O84712; -.
DR SMR; O84712; -.
DR STRING; 813.O172_03900; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; AAC68301; AAC68301; CT_706.
DR GeneID; 884495; -.
DR KEGG; ctr:CT_706; -.
DR PATRIC; fig|272561.5.peg.777; -.
DR HOGENOM; CLU_058707_3_2_0; -.
DR InParanoid; O84712; -.
DR OMA; RDYWMKA; -.
DR Proteomes; UP000000431; 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..203
FT /note="ATP-dependent Clp protease proteolytic subunit 2"
FT /id="PRO_0000179536"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6X60"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:6X60"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:6X60"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6X60"
FT HELIX 140..158
FT /evidence="ECO:0007829|PDB:6X60"
FT HELIX 162..169
FT /evidence="ECO:0007829|PDB:6X60"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6X60"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:6X60"
SQ SEQUENCE 203 AA; 22049 MW; 225C775D64546558 CRC64;
MTLVPYVVED TGRGERAMDI YSRLLKDRIV MIGQEITEPL ANTVIAQLLF LMSEDPTKDI
QIFINSPGGY ITAGLAIYDT IRFLGCDVNT YCIGQAASMG ALLLSAGTKG KRYALPHSRM
MIHQPSGGII GTSADIQLQA AEILTLKKHL SNILAECTGQ SVEKIIEDSE RDFFMGAEEA
IAYGLIDKVI SSAKETKDKS IAS
