CLPP1_CHLT2
ID CLPP1_CHLT2 Reviewed; 192 AA.
AC B0B803;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 1 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP1 {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=CTL0690;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
RN [2]
RP PROTEIN SEQUENCE OF 2-11.
RA Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M.,
RA Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G.,
RA Pallini V.;
RL Submitted (SEP-1994) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM884176; CAP04129.1; -; Genomic_DNA.
DR RefSeq; WP_009873806.1; NC_010287.1.
DR RefSeq; YP_001654762.1; NC_010287.1.
DR AlphaFoldDB; B0B803; -.
DR SMR; B0B803; -.
DR MEROPS; S14.005; -.
DR EnsemblBacteria; CAP04129; CAP04129; CTL0690.
DR KEGG; ctb:CTL0690; -.
DR PATRIC; fig|471472.4.peg.742; -.
DR HOGENOM; CLU_058707_4_0_0; -.
DR OMA; RFIQPHA; -.
DR Proteomes; UP000000795; 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 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 Cytoplasm; Direct protein sequencing; Hydrolase; Protease; Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..192
FT /note="ATP-dependent Clp protease proteolytic subunit 1"
FT /id="PRO_0000340090"
FT ACT_SITE 92
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT CONFLICT 8
FT /note="H -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21073 MW; 589EF06C344F20EF CRC64;
MPEGEMMHKL QDVIDRKLLD SRRIFFSEPV TEKSAAEAIK KLWYLELTNP GQPIVFVINS
PGGSVDAGFA VWDQIKMISS PLTTVVTGLA ASMGSVLSLC AVPGRRFATP HARIMIHQPS
IGGTITGQAT DLDIHAREIL KTKARIIDVY VEATGQSPEV IEKAIDRDMW MSANEAMEFG
LLDGILFSFN DL
