ID   CTPA_SYNP2              Reviewed;         414 AA.
AC   P42784; B1XIH6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Carboxyl-terminal-processing protease;
DE            EC=3.4.21.102;
DE   AltName: Full=CtpA;
DE   Flags: Precursor;
GN   Name=ctpA; OrderedLocusNames=SYNPCC7002_A0843;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-411.
RX   PubMed=1421151; DOI=10.1007/bf00040607;
RA   Brand S.N., Tan X., Widger W.R.;
RT   "Cloning and sequencing of the petBD operon from the cyanobacterium
RT   Synechococcus sp. PCC 7002.";
RL   Plant Mol. Biol. 20:481-491(1992).
CC   -!- FUNCTION: Cleavage of the 16 C-terminal residues from the D1 precursor
CC       of photosystem II (PSII). This proteolytic processing is necessary to
CC       allow the light-driven assembly of the oxygen-evolving cluster (a
CC       tetranuclear manganese), which is responsible for photosynthetic water
CC       oxidation. {ECO:0000250|UniProtKB:Q55669}.
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: Cellular thylakoid lumen
CC       {ECO:0000250|UniProtKB:O04073}.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44776.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000951; ACA98847.1; -; Genomic_DNA.
DR   EMBL; X63049; CAA44776.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; P42784; -.
DR   SMR; P42784; -.
DR   STRING; 32049.SYNPCC7002_A0843; -.
DR   MEROPS; S41.008; -.
DR   EnsemblBacteria; ACA98847; ACA98847; SYNPCC7002_A0843.
DR   KEGG; syp:SYNPCC7002_A0843; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_017295_0_0_3; -.
DR   OMA; DPHSSYY; -.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0031979; C:plasma membrane-derived 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; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   Pfam; PF00595; PDZ; 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   Hydrolase; Protease; Reference proteome; Serine protease; Signal;
KW   Thylakoid.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..414
FT                   /note="Carboxyl-terminal-processing protease"
FT                   /id="PRO_0000207201"
FT   DOMAIN          100..184
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        310
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        321
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        335
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  45575 MW;  A8C2A2542315B488 CRC64;
     MLRKRLQAGL CSLLLVLVLV FGPMERAIAF TDEQDLLLQA WRYVSQAYVD ETFNHQNWWL
     IRQKFLKRPL KTRDEAYEAV GEMLALLDDP YTRLLRPEQY RSLKVSTSGE LSGVGLQINV
     NPEVDVLEVI LPLPGSPAEA AGIEAKDQIL AIDGIDTRNI GLEEAAARMR GKKGSTVSLT
     VKSPKTDTVR TVKVTRDTIA LNPVYDKLDE KNGEKVGYIR LNQFSANAKT EIIKSLNQLQ
     KQGADRYVLD LRNNPGGLLQ AGIEIARLWL DQETIVYTVN RQGIFESYSA VGQPLTDAPL
     VVLVNQATAS ASEILAGALQ DNGRAMLVGE KTFGKGLIQS LFELPDGAGM AVTVAKYETP
     LHHDINKLGI MPDEVVPQEP IGYAMMGSET DLQYQAALDL LTQDQAIAQI SQAS