ID CTPA2_ARATH Reviewed; 515 AA. AC O23614; F4JPY6; Q9ZP02; DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-SEP-2017, entry version 130. DE RecName: Full=Carboxyl-terminal-processing peptidase 2, chloroplastic; DE EC=3.4.21.102; DE AltName: Full=D1 C-terminal processing protease 2; DE AltName: Full=Photosystem II D1 protein processing peptidase 2; DE Flags: Precursor; GN Name=CTPA2; OrderedLocusNames=At4g17740; ORFNames=dl4905c, FCAALL.169; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9461215; DOI=10.1038/35140; RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., RA Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., RA Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., RA Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., RA Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., RA Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., RA Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., RA Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., RA Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., RA Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., RA Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of RT Arabidopsis thaliana."; RL Nature 391:485-488(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-505 (ISOFORM 2). RC STRAIN=cv. Columbia; RA Camilleri R.S., Ridley S.M., Thomas P.G., Bowyer J.R.; RT "Molecular cloning and biochemical characterisation of the Arabidopsis RT thaliana D1-processing protease."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP PROTEIN SEQUENCE OF 127-137, AND SUBCELLULAR LOCATION. RX PubMed=11719511; DOI=10.1074/jbc.M108575200; RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P., RA Kieselbach T.; RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana."; RL J. Biol. Chem. 277:8354-8365(2002). RN [7] RP REVIEW. RX PubMed=16895613; DOI=10.1186/1471-2164-7-200; RA Tripathi L.P., Sowdhamini R.; RT "Cross genome comparisons of serine proteases in Arabidopsis and RT rice."; RL BMC Genomics 7:200-200(2006). CC -!- FUNCTION: Protease involved in the C-terminal processing of the CC chloroplastic D1 protein of photosystem II. This proteolytic CC processing is necessary to allow the light-driven assembly of the CC tetranuclear manganese cluster, which is responsible for CC photosynthetic water oxidation. {ECO:0000250|UniProtKB:O04073}. CC -!- CATALYTIC ACTIVITY: The enzyme shows specific recognition of a C- CC terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala CC or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, CC but then cleaves at a variable distance from the C-terminus. A CC typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala- CC Leu-Ala-Ala. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen CC {ECO:0000269|PubMed:11719511}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O23614-1; Sequence=Displayed; CC Name=2; CC IsoId=O23614-2; Sequence=VSP_054872; CC -!- SIMILARITY: Belongs to the peptidase S41A family. {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; Z97344; CAB10554.1; -; Genomic_DNA. DR EMBL; AL161547; CAB78777.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83943.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83944.1; -; Genomic_DNA. DR EMBL; AY054171; AAL06832.1; -; mRNA. DR EMBL; AF424602; AAL11596.1; -; mRNA. DR EMBL; BT006343; AAP21151.1; -; mRNA. DR EMBL; AJ132544; CAA10694.1; -; mRNA. DR PIR; E71447; E71447. DR RefSeq; NP_193509.1; NM_117883.2. [O23614-1] DR RefSeq; NP_849401.1; NM_179070.1. [O23614-2] DR UniGene; At.4498; -. DR UniGene; At.54; -. DR ProteinModelPortal; O23614; -. DR SMR; O23614; -. DR IntAct; O23614; 1. DR STRING; 3702.AT4G17740.1; -. DR MEROPS; S41.002; -. DR iPTMnet; O23614; -. DR PaxDb; O23614; -. DR PRIDE; O23614; -. DR EnsemblPlants; AT4G17740.1; AT4G17740.1; AT4G17740. [O23614-1] DR EnsemblPlants; AT4G17740.2; AT4G17740.2; AT4G17740. [O23614-2] DR GeneID; 827495; -. DR Gramene; AT4G17740.1; AT4G17740.1; AT4G17740. DR Gramene; AT4G17740.2; AT4G17740.2; AT4G17740. DR KEGG; ath:AT4G17740; -. DR Araport; AT4G17740; -. DR TAIR; locus:2129411; AT4G17740. DR eggNOG; ENOG410IEVI; Eukaryota. DR eggNOG; COG0793; LUCA. DR HOGENOM; HOG000038766; -. DR InParanoid; O23614; -. DR KO; K03797; -. DR OMA; TREIDTE; -. DR OrthoDB; EOG09360ERP; -. DR PhylomeDB; O23614; -. DR PRO; PR:O23614; -. DR Proteomes; UP000006548; Chromosome 4. DR Genevisible; O23614; AT. DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:TAIR. DR GO; GO:0009579; C:thylakoid; IDA:TAIR. DR GO; GO:0031977; C:thylakoid lumen; IDA:TAIR. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR CDD; cd07560; Peptidase_S41_CPP; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001478; PDZ. DR InterPro; IPR004447; Peptidase_S41A. DR InterPro; IPR005151; Tail-specific_protease. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF03572; Peptidase_S41; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00245; TSPc; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR TIGRFAMs; TIGR00225; prc; 1. DR PROSITE; PS50106; PDZ; 1. PE 1: Evidence at protein level; KW Alternative splicing; Chloroplast; Complete proteome; KW Direct protein sequencing; Hydrolase; Plastid; Protease; KW Reference proteome; Serine protease; Thylakoid; Transit peptide. FT TRANSIT 1 ? Chloroplast. {ECO:0000255}. FT TRANSIT ? 126 Thylakoid. {ECO:0000269|PubMed:11719511}. FT CHAIN 127 515 Carboxyl-terminal-processing peptidase 2, FT chloroplastic. FT /FTId=PRO_0000429322. FT DOMAIN 198 286 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT ACT_SITE 417 417 Charge relay system. {ECO:0000250}. FT ACT_SITE 442 442 Charge relay system. {ECO:0000250}. FT VAR_SEQ 28 37 Missing (in isoform 2). FT {ECO:0000303|Ref.5}. FT /FTId=VSP_054872. SQ SEQUENCE 515 AA; 55763 MW; 704BE277C41F0F52 CRC64; MEVLASSSLS PISFTKPNKI NPNFSIQVKL WVKQPPKISK ASKFSYARSR SNISRSNAAN PGVVFVCNRF LCVIERNDQR KLSGKVMMKS SVNFRQNLSV ALVRIVSVLL VSSISVVTTD SPPSWGLTEE NLLFLEAWRT IDRAYIDKTF NGQSWFRYRE TALRNEPMNT REETYMAIKK MVATLDDPFT RFLEPGKFKS LRSGTQGAVT GVGLSIGYPT ASDGPPAGLV VISAAPGGPA NRAGILPGDV IQGIDNTTTE TLTIYDAAQM LQGPEGSAVE LAIRSGPETR LLTLTRERVS VNPVKSRLCE LPGSGSNSPK IGYIKLTTFN QNASSAVREA IETLRGNNVN AFVLDLRDNS GGSFPEGIEI AKFWLDKGVI VYICDSRGVR DIYDTDGSNA IATSEPLAVL VNKGTASASE ILAGALKDNK RALVYGEPTY GKGKIQSVFE LSDGSGLAVT VARYETPAHT DIDKVGVTPD HPLPKSFPKD EEAFCGCLKD PTAACYLNQG LLFSR //