ID   CPHE_PSEAG              Reviewed;         417 AA.
AC   Q8KQN8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Cyanophycinase;
DE            EC=3.4.15.6;
DE   AltName: Full=Extracellular CGPase;
DE            Short=CPHEpa;
DE   AltName: Full=Extracellular cyanophycinase;
DE   Flags: Precursor;
GN   Name=cphE;
OS   Pseudomonas anguilliseptica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=53406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=BI;
RX   PubMed=11986309; DOI=10.1074/jbc.m112267200;
RA   Obst M., Oppermann-Sanio F.B., Luftmann H., Steinbuchel A.;
RT   "Isolation of cyanophycin-degrading bacteria, cloning and characterization
RT   of an extracellular cyanophycinase gene (cphE) from Pseudomonas
RT   anguilliseptica strain BI. The cphE gene from P. anguilliseptica BI encodes
RT   a cyanophycinhydrolyzing enzyme.";
RL   J. Biol. Chem. 277:25096-25105(2002).
RN   [2]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14715021; DOI=10.1021/bm034281p;
RA   Obst M., Sallam A., Luftmann H., Steinbuchel A.;
RT   "Isolation and characterization of gram-positive cyanophycin-degrading
RT   bacteria-kinetic studies on cyanophycin depolymerase activity in aerobic
RT   bacteria.";
RL   Biomacromolecules 5:153-161(2004).
CC   -!- FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi-
CC       L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve
CC       polymer) into aspartate-arginine dipeptides.
CC       {ECO:0000269|PubMed:11986309, ECO:0000269|PubMed:14715021}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-
CC         2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspartate;
CC         Xref=Rhea:RHEA:12845, Rhea:RHEA-COMP:13728, Rhea:RHEA-COMP:13734,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:137986, ChEBI:CHEBI:137991;
CC         EC=3.4.15.6;
CC   -!- ACTIVITY REGULATION: Inhibited by serine protease inhibitors. Inhibited
CC       by N-Bromo-succinimide. {ECO:0000269|PubMed:11986309}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.0 uM for cyanophycin granule polypeptide (CGP)
CC         {ECO:0000269|PubMed:14715021};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11986309}.
CC   -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000305}.
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DR   EMBL; AY065671; AAL40891.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KQN8; -.
DR   SMR; Q8KQN8; -.
DR   KEGG; ag:AAL40891; -.
DR   BRENDA; 3.4.15.6; 8025.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005320; Peptidase_S51.
DR   InterPro; IPR011811; Peptidase_S51_cyanophycinase.
DR   Pfam; PF03575; Peptidase_S51; 1.
DR   PIRSF; PIRSF032067; Cyanophycinase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Secreted; Serine protease; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..417
FT                   /note="Cyanophycinase"
FT                   /id="PRO_0000393371"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  44767 MW;  103788BDFFA2EDE6 CRC64;
     MIRSFIRSSA LLLALLPVTG YSAGPLILVG GGLKDDNTAI YQRLIQLAGG NGQARIGVIT
     AASIPESDDP DAGTADAANS KANGEFYAQL LETYGAADAQ WIPIDLDQIS NNSNPQVVAQ
     INSMTGFFFG GGDQSRLTQT LQTATRADSP ALAAIRARHN AGAVLAGTSA GTAIMVQGPM
     VTGGESYDGL RYGVYTTPSG DDLSYDMQGG FGFFNYGLLD THFSERGRQG RIVRLADHTQ
     VPFAFGVDEN TALLVQNNAT LGQVEMEVIG ENGVFIFDLR NKERGTGSTY ALYDVLGSYL
     TAGDRYRPVT GQFVIASGKT SLRGRERYSA AMTVTTDIFS SPNNSGANGR RKPREFVKVS
     ADLFDSRVTS TLGRTYETNP LSRRSVQKHA VRQPWLPGHR WRQEHAVLPA FADGFPS