CTPA_TETOB
ID CTPA_TETOB Reviewed; 464 AA.
AC O04073;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=C-terminal processing peptidase, chloroplastic;
DE EC=3.4.21.102;
DE AltName: Full=D1 C-terminal processing protease;
DE AltName: Full=Photosystem II D1 protein processing peptidase;
DE Flags: Precursor;
GN Name=ctpA; Synonyms=D1P;
OS Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-113; 155-174; 282-301;
RP 347-368; 399-408 AND 430-452, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=D3;
RX PubMed=9252339; DOI=10.1074/jbc.272.33.20348;
RA Trost J.T., Chisholm D.A., Jordan D.B., Diner B.A.;
RT "The D1 C-terminal processing protease of photosystem II from Scenedesmus
RT obliquus. Protein purification and gene characterization in wild type and
RT processing mutants.";
RL J. Biol. Chem. 272:20348-20356(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 78-464, SUBUNIT, AND ACTIVE SITE.
RX PubMed=10966643; DOI=10.1038/78973;
RA Liao D.I., Qian J., Chisholm D.A., Jordan D.B., Diner B.A.;
RT "Crystal structures of the photosystem II D1 C-terminal processing
RT protease.";
RL Nat. Struct. Biol. 7:749-753(2000).
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:0000269|PubMed:9252339}.
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; Evidence={ECO:0000303|PubMed:9252339};
CC -!- ACTIVITY REGULATION: Not inhibited by antipain, 4-
CC amidinophenylmethanesulfonyl fluoride, aprotinin, chymostatin, 3,4-
CC dichloroisocoumarin, diisopropyl fluorophosphate, E64, EDTA, EGTA,
CC iodoacetamide, leupeptin, pepstatin, o-phenanthroline, N-
CC ethylmaleimide, phosphoramidon or phenylmethylsulfonyl fluoride.
CC {ECO:0000269|PubMed:9252339}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.2. {ECO:0000269|PubMed:9252339};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10966643}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000303|PubMed:9252339}.
CC -!- DISRUPTION PHENOTYPE: The LF-1 strain contains a frameshift causing a
CC premature stop codon within ctpA. This strain is unable to process the
CC precursor form of D1. {ECO:0000305|PubMed:9252339}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR EMBL; U85200; AAC49799.1; -; mRNA.
DR PIR; T10500; T10500.
DR PDB; 1FC6; X-ray; 1.80 A; A=78-464.
DR PDB; 1FC7; X-ray; 2.00 A; A=78-464.
DR PDB; 1FC9; X-ray; 1.90 A; A=78-464.
DR PDB; 1FCF; X-ray; 2.10 A; A=78-464.
DR PDBsum; 1FC6; -.
DR PDBsum; 1FC7; -.
DR PDBsum; 1FC9; -.
DR PDBsum; 1FCF; -.
DR AlphaFoldDB; O04073; -.
DR SMR; O04073; -.
DR MEROPS; S41.002; -.
DR KEGG; ag:AAC49799; -.
DR EvolutionaryTrace; O04073; -.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
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 3D-structure; Chloroplast; Direct protein sequencing; Hydrolase; Plastid;
KW Protease; Serine protease; Thylakoid; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 33..77
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:9252339"
FT CHAIN 78..464
FT /note="C-terminal processing peptidase, chloroplastic"
FT /id="PRO_0000419746"
FT DOMAIN 149..234
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10966643"
FT ACT_SITE 397
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:10966643"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1FCF"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 411..420
FT /evidence="ECO:0007829|PDB:1FC6"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:1FC6"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:1FC6"
FT HELIX 447..455
FT /evidence="ECO:0007829|PDB:1FC6"
SQ 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
