CLPP2_PSEAE
ID CLPP2_PSEAE Reviewed; 201 AA.
AC Q9HYR9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=PA3326;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG06714.1; -; Genomic_DNA.
DR PIR; B83229; B83229.
DR RefSeq; NP_252016.1; NC_002516.2.
DR RefSeq; WP_003091706.1; NZ_QZGE01000017.1.
DR PDB; 7M1L; X-ray; 2.00 A; A/B/C/D/E/F/G=1-201.
DR PDBsum; 7M1L; -.
DR AlphaFoldDB; Q9HYR9; -.
DR SMR; Q9HYR9; -.
DR STRING; 287.DR97_4601; -.
DR PaxDb; Q9HYR9; -.
DR PRIDE; Q9HYR9; -.
DR EnsemblBacteria; AAG06714; AAG06714; PA3326.
DR GeneID; 882491; -.
DR KEGG; pae:PA3326; -.
DR PATRIC; fig|208964.12.peg.3484; -.
DR PseudoCAP; PA3326; -.
DR HOGENOM; CLU_058707_4_0_6; -.
DR InParanoid; Q9HYR9; -.
DR OMA; RFIQPHA; -.
DR PhylomeDB; Q9HYR9; -.
DR BioCyc; PAER208964:G1FZ6-3390-MON; -.
DR Proteomes; UP000002438; 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 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.
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 2"
FT /id="PRO_0000179627"
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 15..27
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 133..158
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:7M1L"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7M1L"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:7M1L"
SQ SEQUENCE 201 AA; 22142 MW; 1188EEF00D6F9AFE CRC64;
MKTDDKDREG GDSHGAIGAK LMEYALKVRK VFVTGGVDEK MAKDVVQQLH ILASISDDPI
YMFVNSPGGH VESGDMIFDA IRFITPKVIM IGSGSVASAG ALIYAAADKE NRYSLPNTRF
LLHQPSGGIQ GPASNIEIYR REIVRMKERL DRIFAEATGQ TPEKISADTE RDFWLNAEEA
VQYGLVNKII VSEREITLPG Q
