CLPP_MAIZE
ID CLPP_MAIZE Reviewed; 216 AA.
AC P26567;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 123.
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};
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-216.
RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf;
RX PubMed=1732000; DOI=10.1007/bf00034970;
RA Wegloehner W., Subramanian A.R.;
RT "Nucleotide sequence of a region of maize chloroplast DNA containing the 3'
RT end of clpP, exon 1 of rps12 and rpl20 and their cotranscription.";
RL Plant Mol. Biol. 18:415-418(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-216.
RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf;
RX PubMed=2822717; DOI=10.1016/s0021-9258(18)48167-7;
RA Giese K., Subramanian A.R., Larrinua I.M., Bogorad L.;
RT "Nucleotide sequence, promoter analysis, and linkage mapping of the
RT unusually organized operon encoding ribosomal proteins S7 and S12 in maize
RT chloroplast.";
RL J. Biol. Chem. 262:15251-15255(1987).
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: Component of the chloroplastic Clp protease core complex.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
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DR EMBL; X86563; CAA60310.1; -; Genomic_DNA.
DR EMBL; X60548; CAA43038.1; -; Genomic_DNA.
DR EMBL; M17842; AAA85358.1; -; Genomic_DNA.
DR PIR; S58576; S58576.
DR RefSeq; NP_043048.1; NC_001666.2.
DR AlphaFoldDB; P26567; -.
DR SMR; P26567; -.
DR STRING; 4577.GRMZM5G804708_P01; -.
DR MEROPS; S14.002; -.
DR PaxDb; P26567; -.
DR PRIDE; P26567; -.
DR GeneID; 845176; -.
DR KEGG; zma:845176; -.
DR MaizeGDB; 67210; -.
DR eggNOG; KOG0840; Eukaryota.
DR HOGENOM; CLU_058707_4_2_1; -.
DR OMA; FPHARVM; -.
DR OrthoDB; 1274502at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR ExpressionAtlas; P26567; baseline.
DR Genevisible; P26567; ZM.
DR GO; GO:0009570; C:chloroplast stroma; 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 3: Inferred from homology;
KW Chloroplast; Hydrolase; Plastid; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..216
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179743"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 126
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 216 AA; 24759 MW; F85B11C5A4D48159 CRC64;
MPIGVPKVPY RIPGDEEATW VDLYNVMYRE RTLFLGQEIR CEITNHITGL MVYLSIEDGN
SDIFLFINSL GGWLISGMAI FDTMQTVTPD IYTICLGIAA SMASFILLGG EPTKRIAFPH
ARIMLHQPAS AYYRARTPEF LLEVEELHKV REMITRVYAL RTGKPFWVVS EDMERDVFMS
ADEAKAYGLV DIVGDEMIDE HCDTDPVWFP EMFKDW
