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

 CTPA_TETOB              Reviewed;         464 AA.
O04073;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
05-DEC-2018, entry version 82.
RecName: Full=C-terminal processing peptidase, chloroplastic;
EC=3.4.21.102;
AltName: Full=D1 C-terminal processing protease;
AltName: Full=Photosystem II D1 protein processing peptidase;
Flags: Precursor;
Name=ctpA; Synonyms=D1P;
Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; Sphaeropleales;
Scenedesmaceae; Tetradesmus.
NCBI_TaxID=3088;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-113; 155-174;
282-301; 347-368; 399-408 AND 430-452, FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=D3;
PubMed=9252339; DOI=10.1074/jbc.272.33.20348;
Trost J.T., Chisholm D.A., Jordan D.B., Diner B.A.;
"The D1 C-terminal processing protease of photosystem II from
Scenedesmus obliquus. Protein purification and gene characterization
in wild type and processing mutants.";
J. Biol. Chem. 272:20348-20356(1997).
[2]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 78-464, SUBUNIT, AND ACTIVE
SITE.
PubMed=10966643; DOI=10.1038/78973;
Liao D.I., Qian J., Chisholm D.A., Jordan D.B., Diner B.A.;
"Crystal structures of the photosystem II D1 C-terminal processing
protease.";
Nat. Struct. Biol. 7:749-753(2000).
-!- 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:0000269|PubMed:9252339}.
-!- CATALYTIC ACTIVITY:
Reaction=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.; EC=3.4.21.102;
Evidence={ECO:0000303|PubMed:9252339};
-!- ACTIVITY REGULATION: Not inhibited by antipain, 4-
amidinophenylmethanesulfonyl fluoride, aprotinin, chymostatin,
3,4-dichloroisocoumarin, diisopropyl fluorophosphate, E64, EDTA,
EGTA, iodoacetamide, leupeptin, pepstatin, o-phenanthroline, N-
ethylmaleimide, phosphoramidon or phenylmethylsulfonyl fluoride.
{ECO:0000269|PubMed:9252339}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.2. {ECO:0000269|PubMed:9252339};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10966643}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
{ECO:0000303|PubMed:9252339}.
-!- DISRUPTION PHENOTYPE: The LF-1 strain contains a frameshift
causing a premature stop codon within ctpA. This strain is unable
to process the precursor form of D1. {ECO:0000305|PubMed:9252339}.
-!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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EMBL; U85200; AAC49799.1; -; mRNA.
PIR; T10500; T10500.
PDB; 1FC6; X-ray; 1.80 A; A=78-464.
PDB; 1FC7; X-ray; 2.00 A; A=78-464.
PDB; 1FC9; X-ray; 1.90 A; A=78-464.
PDB; 1FCF; X-ray; 2.10 A; A=78-464.
PDBsum; 1FC6; -.
PDBsum; 1FC7; -.
PDBsum; 1FC9; -.
PDBsum; 1FCF; -.
ProteinModelPortal; O04073; -.
SMR; O04073; -.
MEROPS; S41.002; -.
PRIDE; O04073; -.
KEGG; ag:AAC49799; -.
KO; K03797; -.
EvolutionaryTrace; O04073; -.
GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
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; PF03572; Peptidase_S41; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00245; TSPc; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR00225; prc; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Chloroplast; Direct protein sequencing; Hydrolase;
Plastid; Protease; Serine protease; Thylakoid; Transit peptide.
TRANSIT 1 32 Chloroplast. {ECO:0000255}.
TRANSIT 33 77 Thylakoid. {ECO:0000269|PubMed:9252339}.
CHAIN 78 464 C-terminal processing peptidase,
chloroplastic.
/FTId=PRO_0000419746.
DOMAIN 149 234 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COMPBIAS 36 77 Ala-rich.
COMPBIAS 264 267 Poly-Ala.
ACT_SITE 372 372 Charge relay system.
{ECO:0000269|PubMed:10966643}.
ACT_SITE 397 397 Charge relay system.
{ECO:0000269|PubMed:10966643}.
HELIX 80 95 {ECO:0000244|PDB:1FC6}.
HELIX 101 103 {ECO:0000244|PDB:1FC6}.
HELIX 106 116 {ECO:0000244|PDB:1FC6}.
HELIX 122 134 {ECO:0000244|PDB:1FC6}.
STRAND 142 144 {ECO:0000244|PDB:1FC6}.
HELIX 146 154 {ECO:0000244|PDB:1FC6}.
STRAND 156 159 {ECO:0000244|PDB:1FC6}.
STRAND 164 169 {ECO:0000244|PDB:1FC6}.
STRAND 171 173 {ECO:0000244|PDB:1FCF}.
STRAND 177 182 {ECO:0000244|PDB:1FC6}.
HELIX 187 190 {ECO:0000244|PDB:1FC6}.
STRAND 198 202 {ECO:0000244|PDB:1FC6}.
HELIX 212 219 {ECO:0000244|PDB:1FC6}.
STRAND 226 233 {ECO:0000244|PDB:1FC6}.
STRAND 236 246 {ECO:0000244|PDB:1FC6}.
STRAND 255 260 {ECO:0000244|PDB:1FC6}.
HELIX 265 267 {ECO:0000244|PDB:1FC6}.
STRAND 273 275 {ECO:0000244|PDB:1FC6}.
STRAND 277 282 {ECO:0000244|PDB:1FC6}.
HELIX 289 302 {ECO:0000244|PDB:1FC6}.
STRAND 306 311 {ECO:0000244|PDB:1FC6}.
HELIX 320 330 {ECO:0000244|PDB:1FC6}.
STRAND 332 341 {ECO:0000244|PDB:1FC6}.
STRAND 344 350 {ECO:0000244|PDB:1FC6}.
STRAND 358 360 {ECO:0000244|PDB:1FC6}.
STRAND 362 366 {ECO:0000244|PDB:1FC6}.
HELIX 373 383 {ECO:0000244|PDB:1FC6}.
STRAND 386 392 {ECO:0000244|PDB:1FC6}.
STRAND 399 405 {ECO:0000244|PDB:1FC6}.
STRAND 411 420 {ECO:0000244|PDB:1FC6}.
TURN 428 430 {ECO:0000244|PDB:1FC6}.
STRAND 435 437 {ECO:0000244|PDB:1FC6}.
HELIX 447 455 {ECO:0000244|PDB:1FC6}.
SEQUENCE 464 AA; 48615 MW; 4066C7CB7EF9FE27 CRC64;
MHSRTNCLQT SVRAPQPHFR PFTAVKTCRQ RCSTTAAAAK RDQAQEQQPW IQVGLGLAAA
ATAVAVGLGA AALPAQAVTS EQLLFLEAWR AVDRAYVDKS FNGQSWFKLR ETYLKKEPMD
RRAQTYDAIR KLLAVLDDPF TRFLEPSRLA ALRRGTAGSV TGVGLEITYD GGSGKDVVVL
TPAPGGPAEK AGARAGDVIV TVDGTAVKGL SLYDVSDLLQ GEADSQVEVV LHAPGAPSNT
RTLQLTRQKV TINPVTFTTC SNVAAAALPP GAAKQQLGYV RLATFNSNTT AAAQQAFTEL
SKQGVAGLVL DIRNNGGGLF PAGVNVARML VDRGDLVLIA DSQGIRDIYS ADGNSIDSAT
PLVVLVNRGT ASASEVLAGA LKDSKRGLIA GERTFGKGLI QTVVDLSDGS GVAVTVARYQ
TPAGVDINKI GVSPDVQLDP EVLPTDLEGV CRVLGSDAAP RLFG


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