CTPA3_ARATH
ID CTPA3_ARATH Reviewed; 519 AA.
AC F4J3G5; Q9SVY2;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Carboxyl-terminal-processing peptidase 3, chloroplastic;
DE EC=3.4.21.102;
DE AltName: Full=D1 C-terminal processing protease 3;
DE AltName: Full=Photosystem II D1 protein processing peptidase 3;
DE Flags: Precursor;
GN Name=CTPA3; OrderedLocusNames=At3g57680; ORFNames=F15B8.130;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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:0000250|UniProtKB:F4KHG6}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049660; CAB41187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79686.1; -; Genomic_DNA.
DR PIR; T06752; T06752.
DR RefSeq; NP_191327.4; NM_115628.5.
DR AlphaFoldDB; F4J3G5; -.
DR SMR; F4J3G5; -.
DR STRING; 3702.AT3G57680.1; -.
DR MEROPS; S41.A01; -.
DR PaxDb; F4J3G5; -.
DR PRIDE; F4J3G5; -.
DR ProteomicsDB; 220455; -.
DR EnsemblPlants; AT3G57680.1; AT3G57680.1; AT3G57680.
DR GeneID; 824937; -.
DR Gramene; AT3G57680.1; AT3G57680.1; AT3G57680.
DR KEGG; ath:AT3G57680; -.
DR Araport; AT3G57680; -.
DR TAIR; locus:2076626; AT3G57680.
DR eggNOG; ENOG502QQVV; Eukaryota.
DR HOGENOM; CLU_017295_0_0_1; -.
DR InParanoid; F4J3G5; -.
DR OrthoDB; 1370241at2759; -.
DR PRO; PR:F4J3G5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J3G5; baseline and differential.
DR Genevisible; F4J3G5; AT.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Chloroplast; Hydrolase; Plastid; Protease; Reference proteome;
KW Serine protease; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..113
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN 114..519
FT /note="Carboxyl-terminal-processing peptidase 3,
FT chloroplastic"
FT /id="PRO_0000429323"
FT DOMAIN 186..274
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 407
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 432
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 519 AA; 56205 MW; 398C796AA22E93D1 CRC64;
MEKVVTLNHD LPLLHFPNSR KPFSIPSPIL RISSFKRHKK RSCLASSSRL GFYTETKTVS
ESHGVIVDNS TIGRRLLGLA AAVSVAVSLS IFCDSPALAE SLTIAFPVSR AREVTTVQRT
LVEAWGLIRE TFVDPTFNHQ DWDFKLQQTM VEMFPLRSAD AAYGKLKAML STLGDPFTRL
ITPKEYQSFR IGSDGNLQGV GLFINSEPRT GHLVVMSCVE GSPADRAGIH EGEELVEING
EKLDDVDSEA AAQKLRGRVG TFVTIKLKNV NGSGTDSGIR EVKLPRDYIK LSPISSAIIP
HTTPDGRLAK TGYVKLTAFS QTAASDMENA VHEMENQDVQ SYILDLRNNP GGLVRAGLDV
AQLWLDGDET LVYTIDREGV TSPINMINGH AVTHDPLVVL VNEGSASASE ILAGALHDNG
RAILVGNRTF GKGKIQSITE LNDGSALFVT VAKYLSPSLH EIDQVGIAPD VQCTTGMIDS
LTAEIVEKMN SSVPLLEADS CVMVAEHELE ARRSNGTAS
