ID CLPP4_FRACC Reviewed; 238 AA.
AC Q2J9A8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 4 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 4 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP4 {ECO:0000255|HAMAP-Rule:MF_00444};
GN OrderedLocusNames=Francci3_2774;
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / HFP020203 / CcI3;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000249; ABD12134.1; -; Genomic_DNA.
DR RefSeq; WP_011437164.1; NZ_LRTJ01000180.1.
DR AlphaFoldDB; Q2J9A8; -.
DR SMR; Q2J9A8; -.
DR STRING; 106370.Francci3_2774; -.
DR MEROPS; S14.008; -.
DR KEGG; fra:Francci3_2774; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_4_1_11; -.
DR OrthoDB; 9802800at2; -.
DR PhylomeDB; Q2J9A8; -.
DR Proteomes; UP000001937; 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; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR PANTHER; PTHR10381:SF70; ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..238
FT /note="ATP-dependent Clp protease proteolytic subunit 4"
FT /id="PRO_0000236390"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 238 AA; 24987 MW; 11BEBA750A02BB6B CRC64;
MIESFSRLTQ AGPGSPRRAT VQAAASGLGS ADDQVFSRLL ENRIVFLGSV VEDAVANAIS
AKLLLLAAED PAADIYLYIN SPGGSVSAGM AIYDTMQYVG NDVATVALGL AGSMGQFLLC
AGTAGKRYAL PHARIMMHQP HGGIGGTAAD ISIQAEQMLY TKRTLQERIA FHTGQTVEQI
ETDSDRDRWF TAEEAKEYGL VDHVVVRADQ VPSVVSGAGM GLRRAGRTGF GPGGGSGR
//
