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Database: UniProt
Entry: K9XPF1_STAC7
LinkDB: K9XPF1_STAC7
Original site: K9XPF1_STAC7 
ID   K9XPF1_STAC7            Unreviewed;       288 AA.
AC   K9XPF1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719, ECO:0000256|PIRNR:PIRNR032067};
DE            EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115, ECO:0000256|PIRNR:PIRNR032067};
GN   OrderedLocusNames=Sta7437_0314 {ECO:0000313|EMBL:AFZ33926.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC   Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ33926.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:0000256|ARBA:ARBA00002039, ECO:0000256|PIRNR:PIRNR032067}.
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; Evidence={ECO:0000256|ARBA:ARBA00001092,
CC         ECO:0000256|PIRNR:PIRNR032067};
CC   -!- SIMILARITY: Belongs to the peptidase S51 family.
CC       {ECO:0000256|ARBA:ARBA00006534, ECO:0000256|PIRNR:PIRNR032067}.
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DR   EMBL; CP003653; AFZ33926.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9XPF1; -.
DR   STRING; 111780.Sta7437_0314; -.
DR   KEGG; scs:Sta7437_0314; -.
DR   PATRIC; fig|111780.3.peg.324; -.
DR   eggNOG; COG4242; Bacteria.
DR   HOGENOM; CLU_053928_0_0_3; -.
DR   OMA; FMTGGDQ; -.
DR   Proteomes; UP000010473; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03145; GAT1_cyanophycinase; 1.
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   NCBIfam; TIGR02069; cyanophycinase; 1.
DR   PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR   PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR   Pfam; PF03575; Peptidase_S51; 1.
DR   PIRSF; PIRSF032067; Cyanophycinase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:AFZ33926.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR032067};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR032067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|PIRNR:PIRNR032067}.
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT   ACT_SITE        192
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT   ACT_SITE        219
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ   SEQUENCE   288 AA;  31496 MW;  18B933D39FEB8414 CRC64;
     MLQMPTMQNR ETQLQSSYTP ALTKTAILVI GGAEDKVHGR EILHTFFNRS GGSEAVIGII
     PSASREPTII GDRYVQIFEE MGTKYTKVLD VRDRDQGNDS VYLDYVEECT GIFLTGGDQL
     RLCGLLAETP LMDRIITRAQ NHEITVGGTS AGAAVMGYHM IAGGSSGESP NRSLVDMAMG
     LGIIPEILVD QHFHNRNRLA RLLSAIASHS ELLGIGIDED TCAMFESDRT IQVLGKGTVT
     IIDARSMSYT NQSQVKGSEP LSIHNLKLHV LCHGERYDLN SHQALPLK
//
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