ID A8IS47_CHLRE Unreviewed; 282 AA. AC A8IS47; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 25-MAY-2022, entry version 68. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000256|RuleBase:RU003567}; GN Name=CLPR2 {ECO:0000313|EMBL:EDP04400.1}; GN ORFNames=CHLRE_16g682900v5 {ECO:0000313|EMBL:PNW72087.1}, GN CHLREDRAFT_183329 {ECO:0000313|EMBL:EDP04400.1}; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] {ECO:0000313|EMBL:EDP04400.1, ECO:0000313|Proteomes:UP000006906} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}, and CC-503 cw92 mt+ RC {ECO:0000313|EMBL:EDP04400.1}; RX PubMed=17932292; DOI=10.1126/science.1143609; RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M., RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L., RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H., RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M., RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C., RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G., RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C., RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J., RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P., RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R., RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P., RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y., RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L., RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.; RT "The Chlamydomonas genome reveals the evolution of key animal and plant RT functions."; RL Science 318:245-250(2007). RN [2] {ECO:0000313|EMBL:PNW72087.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC-503 cw92 mt+ {ECO:0000313|EMBL:PNW72087.1}; RG Chlamydomonas Annotation Team; RG JGI Annotation Team; RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J., RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L., RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H., RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M., RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.; RT "WGS assembly of Chlamydomonas reinhardtii."; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PDB:7EKO, ECO:0007829|PDB:7EKQ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 33-282. RA Wang N., Wang Y.F., Liu C.M., Cong Y.; RT "The cryo-EM structure of the chloroplast Clp complex reveals an RT interaction with the co-chaperonin complex that inhibits Clp proteolytic RT activity."; RL Submitted (APR-2021) to the PDB data bank. CC -!- SIMILARITY: Belongs to the peptidase S14 family. CC {ECO:0000256|ARBA:ARBA00007039, ECO:0000256|RuleBase:RU003567}. 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; DS496121; EDP04400.1; -; Genomic_DNA. DR EMBL; CM008977; PNW72087.1; -; Genomic_DNA. DR RefSeq; XP_001691910.1; XM_001691858.1. DR PDB; 7EKO; EM; 3.30 A; L=33-282. DR PDB; 7EKQ; EM; 3.60 A; L=33-282. DR STRING; 3055.EDP04400; -. DR EnsemblPlants; PNW72087; PNW72087; CHLRE_16g682900v5. DR GeneID; 5717588; -. DR Gramene; PNW72087; PNW72087; CHLRE_16g682900v5. DR KEGG; cre:CHLRE_16g682900v5; -. DR eggNOG; KOG0840; Eukaryota. DR HOGENOM; CLU_058707_2_2_1; -. DR OMA; ASEMHIE; -. DR OrthoDB; 1274502at2759; -. DR Proteomes; UP000006906; Chromosome 16. 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 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7EKO, ECO:0007829|PDB:7EKQ}; KW Reference proteome {ECO:0000313|Proteomes:UP000006906}. SQ SEQUENCE 282 AA; 31582 MW; E8BE2E0C24B21362 CRC64; MQALNQRPSR ATTKTMASGA YIGVKPAANV VGKKSPQGFW QVTTKQISAA KRSGAPKRKV TTMMPVSVPK VLCRPPGQRQ SEWVDLWEAY TYQKVVFIKE AITEDVANNM IALTLYLDSL DQKRIYYWLN VPGGDVVPTL ALYDTMQYVR SKTATVCYGL CLGMGGFLLT AGGEKGYRFA MPHSILMMHH PSGASRGQAS EMHIESRELV RMRDYLSLLT SNATGQPYDR VIRELSRNKW MDPKQAIEYG MIDKVLTTPM PKMPSTGPSF KFERQNDELI GL //