ID   CLPR_SYNE7              Reviewed;         228 AA.
AC   Q9L4P4; Q31K51;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Putative ATP-dependent Clp protease proteolytic subunit-like;
DE   AltName: Full=Endopeptidase Clp-like;
GN   Name=clpR; OrderedLocusNames=Synpcc7942_2538;
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].
RA   Schelin J.R., Clarke A.K.;
RT   "Cloning and sequencing of additional proteolytic subunits of the ATP-
RT   dependent Clp protease (ClpR and ClpP3) from the cyanobacterium
RT   Synechococcus sp. strain PCC 7942.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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: Has lost the two conserved residues (Ser and His) proposed to
CC       be part of the active site. Therefore it could be inactive.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR   EMBL; AJ132005; CAB81780.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58568.1; -; Genomic_DNA.
DR   RefSeq; WP_011243882.1; NC_007604.1.
DR   AlphaFoldDB; Q9L4P4; -.
DR   SMR; Q9L4P4; -.
DR   STRING; 1140.Synpcc7942_2538; -.
DR   MEROPS; S14.001; -.
DR   PRIDE; Q9L4P4; -.
DR   EnsemblBacteria; ABB58568; ABB58568; Synpcc7942_2538.
DR   KEGG; syf:Synpcc7942_2538; -.
DR   eggNOG; COG0740; Bacteria.
DR   HOGENOM; CLU_058707_5_2_3; -.
DR   OMA; ICDTINY; -.
DR   OrthoDB; 1728970at2; -.
DR   BioCyc; MetaCyc:SYNPCC7942_2538-MON; -.
DR   BioCyc; SYNEL:SYNPCC7942_2538-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..228
FT                   /note="Putative ATP-dependent Clp protease proteolytic
FT                   subunit-like"
FT                   /id="PRO_0000179689"
SQ   SEQUENCE   228 AA;  25326 MW;  608AD45D24E0D850 CRC64;
     MLESIQAVQA PYYGDVSYRT PPPDLPSLLL KERIIYLGMP LFSSDDVKRQ VGFDVTELII
     AQLLYLEFDN PEKPIYFYIN STGTSWYTGD AIGYETEAFA ICDTMRYIKP PVHTICIGQA
     MGTAAMILSG GTPGNRASLP HATIVLNQPR TGAQGQASDI QIRAKEVLAN KRTMLEIFAR
     NTGQDPDRLA RDTDRMLYMT PAQAVEYGLI DRVLDSRKDL PAPLPSFS