CLPP_XANOR
ID CLPP_XANOR Reviewed; 208 AA.
AC Q5H434;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=XOO1033;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(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; AE013598; AAW74287.1; -; Genomic_DNA.
DR RefSeq; WP_002806026.1; NC_006834.1.
DR PDB; 7DFT; X-ray; 1.80 A; A/B/C/D/E/F/G=1-208.
DR PDB; 7DFU; X-ray; 1.90 A; A/B/C/D/E/F/G=1-208.
DR PDBsum; 7DFT; -.
DR PDBsum; 7DFU; -.
DR AlphaFoldDB; Q5H434; -.
DR SMR; Q5H434; -.
DR STRING; 291331.XOO1033; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; AAW74287; AAW74287; XOO1033.
DR KEGG; xoo:XOO1033; -.
DR HOGENOM; CLU_058707_3_2_6; -.
DR OMA; RDYWMKA; -.
DR Proteomes; UP000006735; 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..208
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179721"
FT ACT_SITE 105
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 130
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 147..165
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:7DFT"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:7DFT"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:7DFT"
SQ SEQUENCE 208 AA; 22796 MW; F5C0BE4030238544 CRC64;
MSIVTKALNL VPMVVEQTSR GERAYDIYSR LLKERLIFLV GPIDDHMANV IVAQLLFLEA
DNPEKDISIY INSPGGVVTA GMAIYDTMQY IKPDVSTICV GQAASMGALL LASGAAGKRY
ALPNSRVMIH QPLGGFQGQA TDIDIHAREI LTLRSRLNEI LAKHTGQSLE TIARDTERDN
FKSAVDAQAY GLVDQVLERR PEESIQPS
