CTPA2_ARATH
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 03-AUG-2022, entry version 152.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT 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., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., 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., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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 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 processing
CC is necessary to allow the light-driven assembly of the tetranuclear
CC manganese cluster, which is responsible for photosynthetic water
CC oxidation. {ECO:0000250|UniProtKB:O04073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme shows specific recognition of a C-terminal
CC tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa
CC is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves
CC at a variable distance from the C-terminus. A typical cleavage is
CC -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.;
CC EC=3.4.21.102;
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 AlphaFoldDB; 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 ProteomicsDB; 220372; -. [O23614-1]
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. [O23614-1]
DR Gramene; AT4G17740.2; AT4G17740.2; AT4G17740. [O23614-2]
DR KEGG; ath:AT4G17740; -.
DR Araport; AT4G17740; -.
DR TAIR; locus:2129411; AT4G17740.
DR eggNOG; ENOG502QSWI; Eukaryota.
DR InParanoid; O23614; -.
DR OMA; FNHQNWA; -.
DR OrthoDB; 1370241at2759; -.
DR PhylomeDB; O23614; -.
DR BRENDA; 3.4.21.102; 399.
DR PRO; PR:O23614; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23614; baseline and differential.
DR Genevisible; O23614; AT.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR Pfam; PF17820; PDZ_6; 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; 1.
DR TIGRFAMs; TIGR00225; prc; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing; Hydrolase;
KW Plastid; Protease; Reference proteome; Serine protease; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..126
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 127..515
FT /note="Carboxyl-terminal-processing peptidase 2,
FT chloroplastic"
FT /id="PRO_0000429322"
FT DOMAIN 198..286
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 417
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 442
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT VAR_SEQ 28..37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="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
