CTPA_SYNY3
ID CTPA_SYNY3 Reviewed; 427 AA.
AC Q55669; Q55206;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Carboxyl-terminal-processing protease;
DE EC=3.4.21.102;
DE AltName: Full=CtpA;
DE Flags: Precursor;
GN Name=ctpA; OrderedLocusNames=slr0008;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8034700; DOI=10.1016/s0021-9258(17)32175-0;
RA Shestakov S.V., Anbudurai P.R., Stanbekova G.E., Gadzhiev A., Lind L.K.,
RA Pakrasi H.B.;
RT "Molecular cloning and characterization of the ctpA gene encoding a
RT carboxyl-terminal processing protease. Analysis of a spontaneous
RT photosystem II-deficient mutant strain of the cyanobacterium Synechocystis
RT sp. PCC 6803.";
RL J. Biol. Chem. 269:19354-19359(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8058761; DOI=10.1073/pnas.91.17.8082;
RA Anbudurai P.R., Mor T.S., Ohad I., Shestakov S.V., Pakrasi H.B.;
RT "The ctpA gene encodes the C-terminal processing protease for the D1
RT protein of the photosystem II reaction center complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8082-8086(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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:0000269|PubMed:8034700}.
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:0000303|PubMed:8034700}.
CC -!- DISRUPTION PHENOTYPE: Complete loss of PSII.
CC {ECO:0000269|PubMed:8034700}.
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L25250; AAA21727.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10189.1; -; Genomic_DNA.
DR PIR; A53964; A53964.
DR AlphaFoldDB; Q55669; -.
DR SMR; Q55669; -.
DR IntAct; Q55669; 7.
DR STRING; 1148.1001562; -.
DR MEROPS; S41.008; -.
DR PaxDb; Q55669; -.
DR EnsemblBacteria; BAA10189; BAA10189; BAA10189.
DR KEGG; syn:slr0008; -.
DR eggNOG; COG0793; Bacteria.
DR InParanoid; Q55669; -.
DR OMA; FNHQNWA; -.
DR PhylomeDB; Q55669; -.
DR BRENDA; 3.4.21.102; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0031979; C:plasma membrane-derived 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 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..427
FT /note="Carboxyl-terminal-processing protease"
FT /id="PRO_0000027335"
FT DOMAIN 104..186
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 313
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 338
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 46691 MW; C4EA86A08D2638F5 CRC64;
MGKRTRRFWA LAFSLLMGAL IYLGNTPSAL AFTEEQKLLL QSWRLVNQSY LDETFNHQNW
WLLREKYVKR PLRNREETYT AIEEMLATLD EPFTRLLRPE QYGNLQVTTT GELSGVGLQI
NINPETNQLE IMAPLAGSPA EEAGLQPHDQ ILAIDGVDTQ TLSLDEAAAR MRGPKNTKVS
LEILSAGTEV PQEFTLTRQL ISLSPVAAQL DDSRPGQSVG YIRLSQFSAN AYKEVAHALH
QLEEQGADGY ILDLRNNPGG LLQAGIDIAR LWLPESTIVY TVNRQGTQES FTANGEAATD
RPLVVLVNQG TASASEILAG ALQDNQRATL VGEKTFGKGL IQSLFELSDG AGIAVTVAKY
ETPQHHDIHK LGIMPDEVVE QPLISFAEIT SPADVQYQAA LDLLTGGVAI AHKSSSIPAM
ATAHKPN
