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Carboxyl-terminal-processing peptidase 2, chloroplastic (EC 3.4.21.102) (D1 C-terminal processing protease 2) (Photosystem II D1 protein processing peptidase 2)

 CTPA2_ARATH             Reviewed;         515 AA.
O23614; F4JPY6; Q9ZP02;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-APR-2018, entry version 134.
RecName: Full=Carboxyl-terminal-processing peptidase 2, chloroplastic;
EC=3.4.21.102;
AltName: Full=D1 C-terminal processing protease 2;
AltName: Full=Photosystem II D1 protein processing peptidase 2;
Flags: Precursor;
Name=CTPA2; OrderedLocusNames=At4g17740; ORFNames=dl4905c, FCAALL.169;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-505 (ISOFORM 2).
STRAIN=cv. Columbia;
Camilleri R.S., Ridley S.M., Thomas P.G., Bowyer J.R.;
"Molecular cloning and biochemical characterisation of the Arabidopsis
thaliana D1-processing protease.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 127-137, AND SUBCELLULAR LOCATION.
PubMed=11719511; DOI=10.1074/jbc.M108575200;
Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
Kieselbach T.;
"Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
J. Biol. Chem. 277:8354-8365(2002).
[7]
REVIEW.
PubMed=16895613; DOI=10.1186/1471-2164-7-200;
Tripathi L.P., Sowdhamini R.;
"Cross genome comparisons of serine proteases in Arabidopsis and
rice.";
BMC Genomics 7:200-200(2006).
-!- FUNCTION: Protease involved in the C-terminal processing of the
chloroplastic D1 protein of photosystem II. This proteolytic
processing is necessary to allow the light-driven assembly of the
tetranuclear manganese cluster, which is responsible for
photosynthetic water oxidation. {ECO:0000250|UniProtKB:O04073}.
-!- CATALYTIC ACTIVITY: The enzyme shows specific recognition of a C-
terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala
or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala,
but then cleaves at a variable distance from the C-terminus. A
typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-
Leu-Ala-Ala.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
{ECO:0000269|PubMed:11719511}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O23614-1; Sequence=Displayed;
Name=2;
IsoId=O23614-2; Sequence=VSP_054872;
-!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z97344; CAB10554.1; -; Genomic_DNA.
EMBL; AL161547; CAB78777.1; -; Genomic_DNA.
EMBL; CP002687; AEE83943.1; -; Genomic_DNA.
EMBL; CP002687; AEE83944.1; -; Genomic_DNA.
EMBL; AY054171; AAL06832.1; -; mRNA.
EMBL; AF424602; AAL11596.1; -; mRNA.
EMBL; BT006343; AAP21151.1; -; mRNA.
EMBL; AJ132544; CAA10694.1; -; mRNA.
PIR; E71447; E71447.
RefSeq; NP_193509.1; NM_117883.2. [O23614-1]
RefSeq; NP_849401.1; NM_179070.1. [O23614-2]
UniGene; At.4498; -.
UniGene; At.54; -.
ProteinModelPortal; O23614; -.
SMR; O23614; -.
IntAct; O23614; 1.
STRING; 3702.AT4G17740.1; -.
MEROPS; S41.002; -.
iPTMnet; O23614; -.
PaxDb; O23614; -.
PRIDE; O23614; -.
EnsemblPlants; AT4G17740.1; AT4G17740.1; AT4G17740. [O23614-1]
EnsemblPlants; AT4G17740.2; AT4G17740.2; AT4G17740. [O23614-2]
GeneID; 827495; -.
Gramene; AT4G17740.1; AT4G17740.1; AT4G17740. [O23614-1]
Gramene; AT4G17740.2; AT4G17740.2; AT4G17740. [O23614-2]
KEGG; ath:AT4G17740; -.
Araport; AT4G17740; -.
TAIR; locus:2129411; AT4G17740.
eggNOG; ENOG410IEVI; Eukaryota.
eggNOG; COG0793; LUCA.
HOGENOM; HOG000038766; -.
InParanoid; O23614; -.
KO; K03797; -.
OMA; TREIDTE; -.
OrthoDB; EOG09360ERP; -.
PhylomeDB; O23614; -.
PRO; PR:O23614; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; O23614; baseline and differential.
Genevisible; O23614; AT.
GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0031977; C:thylakoid lumen; IDA:TAIR.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
CDD; cd07560; Peptidase_S41_CPP; 1.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR004447; Peptidase_S41A.
InterPro; IPR005151; Tail-specific_protease.
Pfam; PF00595; PDZ; 1.
Pfam; PF03572; Peptidase_S41; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00245; TSPc; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52096; SSF52096; 2.
TIGRFAMs; TIGR00225; prc; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
Alternative splicing; Chloroplast; Complete proteome;
Direct protein sequencing; Hydrolase; Plastid; Protease;
Reference proteome; Serine protease; Thylakoid; Transit peptide.
TRANSIT 1 ? Chloroplast. {ECO:0000255}.
TRANSIT ? 126 Thylakoid. {ECO:0000269|PubMed:11719511}.
CHAIN 127 515 Carboxyl-terminal-processing peptidase 2,
chloroplastic.
/FTId=PRO_0000429322.
DOMAIN 198 286 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
ACT_SITE 417 417 Charge relay system. {ECO:0000250}.
ACT_SITE 442 442 Charge relay system. {ECO:0000250}.
VAR_SEQ 28 37 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_054872.
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


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