CLPP2_SYNE7
ID CLPP2_SYNE7 Reviewed; 240 AA.
AC O34125; Q31K64; Q8GIU2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
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};
GN OrderedLocusNames=Synpcc7942_2525; ORFNames=seb0002;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12101312; DOI=10.1099/00221287-148-7-2255;
RA Schelin J., Lindmark F., Clarke A.K.;
RT "The clpP multigene family for the ATP-dependent Clp protease in the
RT cyanobacterium Synechococcus.";
RL Microbiology 148:2255-2265(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Socias T., Mohler B.J., Chen Y., Min H., Golden S.S.,
RA Youderian P., Sandoval P., Gonzalez A., Salinas I.;
RT "Synechococcus elongatus PCC7942 genome sequence, cosmid 7H1 and 2E8.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=ABB58555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; U92039; AAB68677.1; -; Genomic_DNA.
DR EMBL; U30252; AAL03914.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58555.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011243894.1; NC_007604.1.
DR AlphaFoldDB; O34125; -.
DR SMR; O34125; -.
DR STRING; 1140.Synpcc7942_2525; -.
DR MEROPS; S14.001; -.
DR PRIDE; O34125; -.
DR EnsemblBacteria; ABB58555; ABB58555; Synpcc7942_2525.
DR KEGG; syf:Synpcc7942_2525; -.
DR eggNOG; COG0740; Bacteria.
DR HOGENOM; CLU_058707_3_2_3; -.
DR OrthoDB; 1728970at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_2525-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_2525-MON; -.
DR BRENDA; 3.4.21.92; 6187.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Serine protease.
FT CHAIN 1..240
FT /note="ATP-dependent Clp protease proteolytic subunit 2"
FT /id="PRO_0000179687"
FT ACT_SITE 132
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 157
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
SQ SEQUENCE 240 AA; 25987 MW; 865EA0FC3F7600F6 CRC64;
MFSSHASLPI HSRRLAAGLD SRWQQPQIQA IAGSQAIVPT VVEQSGRGER AFDIYSRLLR
ERIVFLGTGV DDAVADSIVA QLLFLEAEDP EKDIQLYINS PGGSVTAGMA IYDTMQQVAP
DVATICFGLA ASMGAFLLSG GAQGKRMALP SARIMIHQPL GGAQGQAVDI EIQAREILYH
KSTLNDLLAQ HTGQPLEKIE VDTDRDFFMS PEEAKAYGLI DQVLTRPTMA ITDHNDAVLQ
