ID   CPHB_NOSS1              Reviewed;         298 AA.
AC   P58562;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cyanophycinase;
DE            EC=3.4.15.6;
GN   Name=cphB; OrderedLocusNames=all3880;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75579.1; -; Genomic_DNA.
DR   PIR; AI2290; AI2290.
DR   AlphaFoldDB; P58562; -.
DR   SMR; P58562; -.
DR   STRING; 103690.17133014; -.
DR   EnsemblBacteria; BAB75579; BAB75579; BAB75579.
DR   KEGG; ana:all3880; -.
DR   eggNOG; COG4242; Bacteria.
DR   OMA; FMTGGDQ; -.
DR   Proteomes; UP000002483; Chromosome.
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; Reference proteome; Serine protease.
FT   CHAIN           1..298
FT                   /note="Cyanophycinase"
FT                   /id="PRO_0000209971"
FT   ACT_SITE        155
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        197
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  32363 MW;  9711A945BD8B5917 CRC64;
     MAPKVVDRRN TMPQLQAKSL EMRTPQATKT AVLVIGGAED KVHGREILRT FFGRAGASKA
     YITIIPSASR EPAIIGGRYI RIFEEMGAEK VEILDIRERE QCESSQVKAS LEACSGVFLT
     GGDQLRLCGV LSDTPVMEII RQRVRGGQLT LAGTSAGAAV MGHHMIAGGG SGETPNRSLV
     DMATGLGLIP EVIVDQHFHN RNRMGRLISA VAAHPDRLGI GIDEDTCAVF ERDGWLQVLG
     KGSVTIVDPT ELTHTNEPHV GANEPLTVHN LRLHILSYGD RFHLYQRTVL PAVHRISS