ID   CPHB_SYNEL              Reviewed;         322 AA.
AC   P0C8P2; Q9F2I8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Cyanophycinase;
DE            EC=3.4.15.6;
GN   Name=cphB;
OS   Synechococcus elongatus.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=32046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10951215; DOI=10.1046/j.1432-1327.2000.01622.x;
RA   Berg H., Ziegler K., Piotukh K., Baier K., Lockau W., Volkmer-Engert R.;
RT   "Biosynthesis of the cyanobacterial reserve polymer multi-L-arginyl-poly-L-
RT   aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase
RT   reaction studied with synthetic primers.";
RL   Eur. J. Biochem. 267:5561-5570(2000).
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   -!- 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   -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000305}.
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DR   EMBL; AJ288949; CAC07986.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C8P2; -.
DR   SMR; P0C8P2; -.
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.
DR   TIGRFAMs; TIGR02069; cyanophycinase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Serine protease.
FT   CHAIN           1..322
FT                   /note="Cyanophycinase"
FT                   /id="PRO_0000209973"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        220
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   322 AA;  35503 MW;  8D319403D45245B7 CRC64;
     MLYRIPVSTV GYWHSPWQIH QFLLPIERFI HRNPMLQLDP ISKTTHQHSG HKGLVMAIGG
     AEDKVRGRQI LTTFCQRAGG LDAVIGVIPS ASREPDAMGR LYHDIFRDIG VREVDILLVG
     DRADAEQEEM LARLSRCTGI FMSGGDQLRL SALLDETPLL YQLRHQVWEG KSILGGTSAG
     AAVLGECMIA SGGSNEAPNR SLVDLATGLG ILPDVLVDQH FHNRNRLARL ISAISAHPDK
     LGVGIDEDTC AMFEADGTLR VLGRGSVTIV DPRDVSYTNY AHVDVNEPLS IYNLRLHILS
     DGDCYNLRTH QVQHKCILPP LN